메뉴 건너뛰기




Volumn , Issue , 2018, Pages 1-140

Enzymatic peptide synthesis

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85054372499     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781351071833     Document Type: Book
Times cited : (67)

References (482)
  • 1
    • 84945084007 scopus 로고
    • Über einige Derivate des Glykocolls
    • Fischer, E. and Fourneau, E., Über einige Derivate des Glykocolls, Ber. Dtsch. Chem. Ges., 34, 2868, 1901.
    • (1901) Ber. Dtsch. Chem. Ges. , vol.34 , pp. 2868
    • Fischer, E.1    Fourneau, E.2
  • 2
    • 0000756014 scopus 로고
    • Über die Einwirkung des Chlorobenzoyl auf Glycocollsilber
    • Curtius, T., Über die Einwirkung des Chlorobenzoyl auf Glycocollsilber, J. Prakt. Chem., 24, 239, 1882.
    • (1882) J. Prakt. Chem. , vol.24 , pp. 239
    • Curtius, T.1
  • 5
    • 0001149042 scopus 로고
    • Synthese von Peptiden
    • G. Thieme Verlag, Stuttgart
    • Wünsch, E., Synthese von Peptiden, in Methoden der Organischen Chemie, Vol. 15, Parts 1 and 2, G. Thieme Verlag, Stuttgart, 1974.
    • (1974) Methoden Der Organischen Chemie , vol.15
    • Wünsch, E.1
  • 6
    • 26144456010 scopus 로고
    • Chemie und Biochemie der Aminosären
    • G. Thieme Verlag, Stuttgart
    • Lübke, K., Schröder, E., and Kloss, G., Chemie und Biochemie der Aminosären, Peptide und Proteine, Vols. 1 and 2, G. Thieme Verlag, Stuttgart, 1975.
    • (1975) Peptide Und Proteine , vol.1-2
    • Lübke, K.1    Schröder, E.2    Kloss, G.3
  • 9
    • 0004249010 scopus 로고
    • Principles of peptide synthesis
    • Hafner, K., Rees, C. W., Trost, B. M., Lehn, J.-M., v.Rague-Schleyer, P., and Zahradnik, R., Eds., Springer-Verlag, Berlin
    • Bodanszky, M., Principles of peptide synthesis, in Reactivity and Structure: Concepts in Organic Chemistry, Vol. 16, Hafner, K., Rees, C. W., Trost, B. M., Lehn, J.-M., v.Rague-Schleyer, P., and Zahradnik, R., Eds., Springer-Verlag, Berlin, 1984.
    • (1984) Reactivity and Structure: Concepts in Organic Chemistry , vol.16
    • Bodanszky, M.1
  • 10
    • 0003803058 scopus 로고
    • The practice of peptide synthesis
    • Hafner, K., Rees, C. W., Trost, B. M., Lehn, J.-M., v.Rague-Schleyer, P., and Zahradnik, R., Eds., Springer-Verlag, Berlin
    • Bodanszky, M. and Bodanszky, A., The practice of peptide synthesis, in Reactivity and Structure: Concepts in Organic Chemistry, Vol. 21, Hafner, K., Rees, C. W., Trost, B. M., Lehn, J.-M., v.Rague-Schleyer, P., and Zahradnik, R., Eds., Springer-Verlag, Berlin, 1984.
    • (1984) Reactivity and Structure: Concepts in Organic Chemistry , vol.21
    • Bodanszky, M.1    Bodanszky, A.2
  • 11
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • Merrifield, R. B., Solid phase peptide synthesis. I. The synthesis of a tetrapeptide, J. Am. Chem. Soc., 85, 2149, 1963.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149
    • Merrifield, R.B.1
  • 12
    • 0001120111 scopus 로고
    • Eine neue Methode zur Synthese von Polypeptiden
    • Mutter, M., Hagenmaier, H., and Bayer, E., Eine neue Methode zur Synthese von Polypeptiden, Angew. Chem., 83, 883, 1971.
    • (1971) Angew. Chem. , vol.83 , pp. 883
    • Mutter, M.1    Hagenmaier, H.2    Bayer, E.3
  • 13
    • 0016439313 scopus 로고
    • Ein neues Verfahren zur Peptidsynthese: Die alternierende Fest-Flüssigphasen Methode
    • Frank, H. and Hagenmaier, H., Ein neues Verfahren zur Peptidsynthese: die alternierende Fest-Flüssigphasen Methode, Experientia,31, 131, 1975.
    • (1975) Experientia , vol.31 , pp. 131
    • Frank, H.1    Hagenmaier, H.2
  • 14
    • 85012394492 scopus 로고
    • Peptide synthesis: An undiminished challenge
    • Goodman, M. and Meienhofer, J., Eds., John Wiley and Sons, New York
    • Bodanszky, M., Peptide synthesis: an undiminished challenge, in Peptides, Proc. 5th Am. Peptide Symp., Goodman, M. and Meienhofer, J., Eds., John Wiley and Sons, New York, 1977, 1.
    • (1977) Peptides, Proc. 5Th Am. Peptide Symp , pp. 1
    • Bodanszky, M.1
  • 16
    • 0019508396 scopus 로고
    • Ribosomal components from escherichia coli 50S subunits involved in the reconstitution of peptidyltransferase activity
    • Hampl, H., Schulze, H., and Nierhaus, K. H., Ribosomal components from escherichia coli 50S subunits involved in the reconstitution of peptidyltransferase activity, J. Biol. Chem., 256, 2284, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2284
    • Hampl, H.1    Schulze, H.2    Nierhaus, K.H.3
  • 19
    • 85052487146 scopus 로고
    • Uber die zunehmende Bedeutung der anorganischen Chemie
    • Van’t Hoff, J. H., Uber die zunehmende Bedeutung der anorganischen Chemie, Z. Anorg. Chem., 18, 1, 1898.
    • (1898) Z. Anorg. Chem. , vol.18 , pp. 1
    • Van’T Hoff, J.H.1
  • 20
    • 37049165303 scopus 로고
    • Reversible zymohydrolysis
    • Hill, A. C., Reversible zymohydrolysis, J. Chem. Soc., 73, 634, 1898.
    • (1898) J. Chem. Soc. , vol.73 , pp. 634
    • Hill, A.C.1
  • 21
    • 85023561287 scopus 로고
    • Sur la réversibilité des actions diastasiques
    • Hanriot, M., Sur la réversibilité des actions diastasiques, C.R. Soc. Biol., 53, 70, 1901.
    • (1901) C.R. Soc. Biol. , vol.53 , pp. 70
    • Hanriot, M.1
  • 23
    • 12244301309 scopus 로고
    • Die synthetisierende Wirkung von Fermenten
    • Ammon, R., Die synthetisierende Wirkung von Fermenten, Angew. Chem., 45, 357, 1932.
    • (1932) Angew. Chem. , vol.45 , pp. 357
    • Ammon, R.1
  • 25
    • 0347259956 scopus 로고
    • Nucleotide exchange reactions catalyzed by ribo-nuclease and spleen phosphodiesterase
    • Heppel, L. A., Whitfield, P. R., and Markham, R., Nucleotide exchange reactions catalyzed by ribo-nuclease and spleen phosphodiesterase, Biochem. J., 60, 8, 1955.
    • (1955) Biochem. J. , vol.60 , pp. 8
    • Heppel, L.A.1    Whitfield, P.R.2    Markham, R.3
  • 26
    • 0016296727 scopus 로고
    • Some notes and queries on the development of bioenergetics. Notes on some 'Founding Fathers’ of physical chemistry, J. Willard Gibbs, Wilhelm Ostwald, Walther Nernst, Gilbert Newton Lewis
    • Edsall, J. T., Some notes and queries on the development of bioenergetics. Notes on some 'Founding Fathers’ of physical chemistry, J. Willard Gibbs, Wilhelm Ostwald, Walther Nernst, Gilbert Newton Lewis, Mol. Cell. Biochem., 5, 103, 1974.
    • (1974) Mol. Cell. Biochem. , vol.5 , pp. 103
    • Edsall, J.T.1
  • 28
    • 85052473878 scopus 로고
    • The organoplastic forces of the organism (In Russian)
    • Elsevier, Amsterdam
    • Danilevski, B., The organoplastic forces of the organism (in Russian), in Comprehensive Biochemistry, Vol. 32, Elsevier, Amsterdam, 1977, 314.
    • (1977) Comprehensive Biochemistry , vol.32 , pp. 314
    • Danilevski, B.1
  • 29
    • 84982059488 scopus 로고
    • Untersuchungen über die Plastein-Reaktion. Isolierung einheitlicher Plastein-Bausteine
    • Wieland, T., Deterntann, H., and Albrecht, E., Untersuchungen über die Plastein-Reaktion. Isolierung einheitlicher Plastein-Bausteine., Justus Liebigs Ann. Chem., 633, 185, 1960.
    • (1960) Justus Liebigs Ann. Chem. , vol.633 , pp. 185
    • Wieland, T.1    Deterntann, H.2    Albrecht, E.3
  • 30
    • 0002918033 scopus 로고
    • The enzymatic synthesis of peptide bonds
    • Bergmann, M. and Fraenkel-Conrat, H., The enzymatic synthesis of peptide bonds, J. Biol. Chem., 124, 1, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 1
    • Bergmann, M.1    Fraenkel-Conrat, H.2
  • 31
    • 0343889591 scopus 로고
    • Some synthetic and hydrolytic experiments with Chymotrypsin
    • Bergmann, M., and Fruton, J. S., Some synthetic and hydrolytic experiments with Chymotrypsin., J. Biol. Chem., 124, 321, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 321
    • Bergmann, M.1    Fruton, J.S.2
  • 32
    • 4243463304 scopus 로고
    • The structure of proteins in relation to biological problems
    • Bergmann, M., The structure of proteins in relation to biological problems, Chem. Rev., 22, 423, 1938.
    • (1938) Chem. Rev. , vol.22 , pp. 423
    • Bergmann, M.1
  • 34
    • 39549094386 scopus 로고
    • Proteases as agents in the formation and breakdown of proteins
    • Fruton, J. S., Proteases as agents in the formation and breakdown of proteins, Cold Spring Harbor Symp. Quant. Biol., 9, 211, 1941.
    • (1941) Cold Spring Harbor Symp. Quant. Biol. , vol.9 , pp. 211
    • Fruton, J.S.1
  • 36
    • 1542628195 scopus 로고
    • Peptide bond formation
    • Borsook, H., Peptide bond formation. Adv. Prot. Chem., 8, 127, 1953.
    • (1953) Adv. Prot. Chem. , vol.8 , pp. 127
    • Borsook, H.1
  • 37
    • 0002720053 scopus 로고
    • Metabolic generation and utilization of phosphate bond energy
    • Lipmann, F., Metabolic generation and utilization of phosphate bond energy, Adv. Enzymol. Relat. Subj., 1, 99, 1941.
    • (1941) Adv. Enzymol. Relat. Subj. , vol.1 , pp. 99
    • Lipmann, F.1
  • 38
    • 16944366812 scopus 로고
    • The nature of energetic coupling in biological syntheses
    • Kalckar, H. M., The nature of energetic coupling in biological syntheses, Chem. Rev., 28, 71, 1941.
    • (1941) Chem. Rev. , vol.28 , pp. 71
    • Kalckar, H.M.1
  • 39
    • 33745257181 scopus 로고
    • Enzymic hydrolysis and synthesis of peptide bonds
    • Fruton, J. S., Enzymic hydrolysis and synthesis of peptide bonds, Harvey Lectures 1955,51, 64, 1957.
    • (1957) Harvey Lectures , vol.1955 , Issue.51 , pp. 64
    • Fruton, J.S.1
  • 42
    • 1542628195 scopus 로고
    • Peptide bond formation
    • Borsook, H., Peptide bond formation, Adv. Prot. Chem., 8, 127, 1953.
    • (1953) Adv. Prot. Chem. , vol.8 , pp. 127
    • Borsook, H.1
  • 43
    • 85054394020 scopus 로고
    • Biological synthesis of proteins, Lane medical lectures 1951
    • Academic Press, New York
    • Linderstrom-Lang, K., Biological synthesis of proteins, Lane medical lectures 1951, in Selected Papers, Academic Press, New York, 1962, 448.
    • (1962) Selected Papers , pp. 448
    • Linderstrom-Lang, K.1
  • 44
    • 33947480695 scopus 로고
    • The free energy change in hydrolytic reactions: The non-ionized compound convention
    • Carpenter, F. H., The free energy change in hydrolytic reactions: the non-ionized compound convention, J. Am. Chem. Soc., 82, 1111, 1960.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 1111
    • Carpenter, F.H.1
  • 45
    • 85054398013 scopus 로고
    • On the enzymatic synthesis of peptide bonds
    • Waldschmidt-Leitz, E., On the enzymatic synthesis of peptide bonds, Angew. Chem., 61, 437, 1949.
    • (1949) Angew. Chem. , vol.61 , pp. 437
    • Waldschmidt-Leitz, E.1
  • 46
    • 0039233239 scopus 로고
    • Thermodynamics of hydrolysis of peptide bonds
    • Dobry, A., Fruton, J. S., and Sturtevant, J. M., Thermodynamics of hydrolysis of peptide bonds, J. Biol. Chem., 195, 149, 1952.
    • (1952) J. Biol. Chem. , vol.195 , pp. 149
    • Dobry, A.1    Fruton, J.S.2    Sturtevant, J.M.3
  • 47
    • 0019531170 scopus 로고
    • Studies on protein semisynthesis. I. Formation of esters, hydrazides, and substituted hy-drazides of peptides by the reverse reaction of trypsin
    • Yagisawa, S., Studies on protein semisynthesis. I. Formation of esters, hydrazides, and substituted hy-drazides of peptides by the reverse reaction of trypsin, J. Biochem., 89, 491, 1981.
    • (1981) J. Biochem. , vol.89 , pp. 491
    • Yagisawa, S.1
  • 48
    • 1342296307 scopus 로고
    • The activated complex and the absolute rate of chemical reactions
    • Eyring, H., The activated complex and the absolute rate of chemical reactions, Chem. Rev., 17, 65, 1935.
    • (1935) Chem. Rev. , vol.17 , pp. 65
    • Eyring, H.1
  • 49
    • 2142703660 scopus 로고
    • Entropy, binding energy, and enzymic catalysis
    • Page, M. J., Entropy, binding energy, and enzymic catalysis, Angew. Chem. Int. Ed. Engl., 16, 449, 1977.
    • (1977) Angew. Chem. Int. Ed. Engl. , vol.16 , pp. 449
    • Page, M.J.1
  • 52
    • 0001423787 scopus 로고
    • Nonribosomal polypeptide synthesis on polyenzyme templates
    • Lipmann, F., Nonribosomal polypeptide synthesis on polyenzyme templates, Ace. Chem. Res., 6. 361, 1973.
    • (1973) Ace. Chem. Res. , vol.6 , pp. 361
    • Lipmann, F.1
  • 53
    • 33847799412 scopus 로고
    • Structure and mechanisms of chymotrypsin. Ace
    • Blow, D. M., Structure and mechanisms of chymotrypsin. Ace. Chem. Res., 9. 145, 1976.
    • (1976) Chem. Res. , vol.9 , pp. 145
    • Blow, D.M.1
  • 54
    • 0039895495 scopus 로고
    • Reactivity and catalysis in reactions of the serine hydroxyl group and of O-acyl serines
    • Anderson, B. W., Cordes, E. H., and Jencks, W. P., Reactivity and catalysis in reactions of the serine hydroxyl group and of O-acyl serines, J. Biol. Chem., 236, 455, 1961.
    • (1961) J. Biol. Chem. , vol.236 , pp. 455
    • Anderson, B.W.1    Cordes, E.H.2    Jencks, W.P.3
  • 55
    • 0001781266 scopus 로고
    • The comparison of non-enzymic and enzymic reaction velocities
    • Koshland, D. E., Jr., The comparison of non-enzymic and enzymic reaction velocities, J. Theoret. Biol., 2, 75, 1962.
    • (1962) J. Theoret. Biol. , vol.2 , pp. 75
    • Koshland, D.E.1
  • 56
    • 77956910473 scopus 로고
    • Trypsin
    • 3rd ed. Part III, Boyer, P. D., Ed., Academic Press, New York
    • Keil, B., Trypsin, in The Enzymes,3rd ed. Part III, Boyer, P. D., Ed., Academic Press, New York, 1971, 249.
    • (1971) The Enzymes , pp. 249
    • Keil, B.1
  • 57
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber, R. and Bode, W., Structural basis of the activation and action of trypsin, Aec. Chem. Res.11, 114, 1978.
    • (1978) Aec. Chem. Res. , vol.11 , pp. 114
    • Huber, R.1    Bode, W.2
  • 58
    • 0015497445 scopus 로고
    • Subtilisin; a stereochemical mechanism involving transition-state stabilization
    • Robertus, J. D., Kraut, J., Alden, R. A., and Birktoft, J. J., Subtilisin; a stereochemical mechanism involving transition-state stabilization, Biochemistry, 11, 4293, 1972.
    • (1972) Biochemistry , vol.11 , pp. 4293
    • Robertus, J.D.1    Kraut, J.2    Alden, R.A.3    Birktoft, J.J.4
  • 59
    • 0347806804 scopus 로고
    • Direct observation of transient ES complexes: Implications to enzyme mechanisms
    • van Tamelen, E. E., Ed., Academic Press. New York
    • Auld, D. S., Direct observation of transient ES complexes: implications to enzyme mechanisms, in Bioor-ganic Chemistry, Vol. 1, van Tamelen, E. E., Ed., Academic Press. New York, 1977. 1.
    • (1977) Bioor-Ganic Chemistry , vol.1 , pp. 1
    • Auld, D.S.1
  • 60
    • 0001703784 scopus 로고
    • The kinetics and mechanisms of papain-catalyzed hydrolysis
    • Bender, K. L. and Brubacher, L. J., The kinetics and mechanisms of papain-catalyzed hydrolysis, J. Am. Chem. Soc., 88, 5880, 1966.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 5880
    • Bender, K.L.1    Brubacher, L.J.2
  • 61
    • 3643111814 scopus 로고
    • The cysteine proteinases
    • Lowe, G., The cysteine proteinases. Tetrahedron,32, 291, 1976.
    • (1976) Tetrahedron , vol.32 , pp. 291
    • Lowe, G.1
  • 62
    • 0002939999 scopus 로고
    • Acyl- and amino-transler routes in pepsin-catalyzed reactions
    • Newmark, A. K. and Knowles, J. R., Acyl- and amino-transler routes in pepsin-catalyzed reactions. J. Am. Chem. Soc.97. 3557. 1975.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 3557
    • Newmark, A.K.1    Knowles, J.R.2
  • 63
    • 0016755859 scopus 로고
    • Acyl intermediates in penicillopepsin-catalyzed reactions and a discussion of the mechanisms of action of pepsins
    • Takahashi, M. and Hofmann, T., Acyl intermediates in penicillopepsin-catalyzed reactions and a discussion of the mechanisms of action of pepsins, Biochem. J.147. 549, 1975.
    • (1975) Biochem. J. , vol.147 , pp. 549
    • Takahashi, M.1    Hofmann, T.2
  • 64
    • 0017262478 scopus 로고
    • Effects of secondary binding by activator peptides on covalent intermediates of pig pepsin
    • Wang, T.-T. and Hofmann, T., Effects of secondary binding by activator peptides on covalent intermediates of pig pepsin, Biochem. J., 153. 701, 1976.
    • (1976) Biochem. J. , vol.153 , pp. 701
    • Wang, T.-T.1    Hofmann, T.2
  • 65
    • 33947088124 scopus 로고
    • Carboxypeptidase A: A mechanistic analysis
    • Kaiser, B. L. and Kaiser, E. T., Carboxypeptidase A: a mechanistic analysis, Acc. Chem. Res.5. 219. 1972.
    • (1972) Acc. Chem. Res. , vol.5 , pp. 219
    • Kaiser, B.L.1    Kaiser, E.T.2
  • 67
    • 0018082849 scopus 로고
    • Acyl and amino intermediates in reactions catalyzed by thermolysin
    • Morihara, K., Tsuzuki, H., and Oka, T., Acyl and amino intermediates in reactions catalyzed by thermolysin, Biochem. Biophys. Res. Commutt.84, 95. 1978.
    • (1978) Biochem. Biophys. Res. Commutt. , vol.84 , pp. 95
    • Morihara, K.1    Tsuzuki, H.2    Oka, T.3
  • 68
    • 0017379736 scopus 로고
    • A-Chymotrypsin as the catalyst for peptide synthesis
    • Morihara, K., and Oka, T., a-Chymotrypsin as the catalyst for peptide synthesis, Biochem. J.163. 531. 1977.
    • (1977) Biochem. J. , vol.163 , pp. 531
    • Morihara, K.1    Oka, T.2
  • 69
    • 33947480695 scopus 로고
    • The free energy change in hydrolytic reactions: The non-ionized compound convention
    • Carpenter, F. H., The free energy change in hydrolytic reactions: The non-ionized compound convention, J. Am. Chem. Soc.82, 1111, 1960.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 1111
    • Carpenter, F.H.1
  • 70
    • 0006272112 scopus 로고
    • Die Dissoziation der schwachen Elektrolyte in wässrig-alkoholischen Lösungen, Z
    • Michaelis, L. and Mizutani, M., Die Dissoziation der schwachen Elektrolyte in wässrig-alkoholischen Lösungen, Z. Phys. Chem. (Leipzig),116, 135, 1925.
    • (1925) Phys. Chem. (Leipzig) , vol.116 , pp. 135
    • Michaelis, L.1    Mizutani, M.2
  • 71
    • 0006344792 scopus 로고
    • Die Dissoziation der schwachen Elektrolyte in wässrig-alkoholischen Lösungen. Die Beziehungen zwischen chemischer Konstitution und Alkoholempfindlichkeit der Säuren und Basen, Z
    • Mizutani, M., Die Dissoziation der schwachen Elektrolyte in wässrig-alkoholischen Lösungen. Die Beziehungen zwischen chemischer Konstitution und Alkoholempfindlichkeit der Säuren und Basen, Z. Phys. Chem.(Leipzig).116, 350, 1925.
    • (1925) Phys. Chem.(Leipzig) , vol.116 , pp. 350
    • Mizutani, M.1
  • 72
    • 0018278636 scopus 로고
    • Synthesis of peptide bonds by proteinases. Addition of cosolvents shifts peptide bond equilibria toward synthesis
    • Homandberg, G. A., Mattis, J. A., and Laskovski, M., Jr., Synthesis of peptide bonds by proteinases. Addition of cosolvents shifts peptide bond equilibria toward synthesis. Biochemistry',17, 5220, 1978.
    • (1978) Biochemistry , vol.17 , pp. 5220
    • Homandberg, G.A.1    Mattis, J.A.2    Laskovski, M.3
  • 73
    • 85052780222 scopus 로고
    • The principle of formaldehyde, alcohol, and acetone titrations. With a discussion of the proof and implication of the zwitterionic conception
    • Richardson, G. M., The principle of formaldehyde, alcohol, and acetone titrations. With a discussion of the proof and implication of the zwitterionic conception, Proc. R. Stic. London B.115, 121. 1934.
    • (1934) Proc. R. Stic. London B , vol.115 , pp. 121
    • Richardson, G.M.1
  • 74
    • 84970582475 scopus 로고
    • The effect of temperature on pK values of organic bases
    • Perrin, D. D., The effect of temperature on pK values of organic bases. Aus. J. Chem.17, 484. 1964.
    • (1964) Aus. J. Chem. , vol.17 , pp. 484
    • Perrin, D.D.1
  • 75
    • 0019964097 scopus 로고
    • Proteasen als Biokatalysatoren fur die Peptidsynthese
    • Jakubke, H.-D. and Kuhl, P., Proteasen als Biokatalysatoren fur die Peptidsynthese. Phannazie.37, 89. 1982.
    • (1982) Phannazie , vol.37 , pp. 89
    • Jakubke, H.-D.1    Kuhl, P.2
  • 76
    • 0006880052 scopus 로고    scopus 로고
    • The use of proteolytic enzy mes for the sy nthesis of specific peptide bonds in globular proteins
    • Offord, R. E. and DiBello. C. Eds., Academic Press. New York, 1978, 25.5
    • Laskowski, M., Jr., The use of proteolytic enzy mes for the sy nthesis of specific peptide bonds in globular proteins, in Semisynthetic Peptides and Proteins. Offord, R. E. and DiBello. C. Eds., Academic Press. New York, 1978, 25.5.
    • Semisynthetic Peptides and Proteins
    • Laskowski, M.1
  • 77
    • 0002918033 scopus 로고
    • The enzymatic synthesis of peptide bonds
    • Bergmann, M. and Fraenkel-Conrat, H., The enzymatic synthesis of peptide bonds, /. Biol. Chem. 124, 1, 1938.
    • (1938) Biol. Chem. , vol.124 , pp. 1
    • Bergmann, M.1    Fraenkel-Conrat, H.2
  • 78
    • 0343889591 scopus 로고
    • Some synthetic and hydrolytic experiments with chymotrypsin
    • Bergmann, M. and Fruton, J. S., Some synthetic and hydrolytic experiments with chymotrypsin., J. Biol. Chem.124, 321, 1938.
    • (1938) J. Biol. Chem , vol.124 , pp. 321
    • Bergmann, M.1    Fruton, J.S.2
  • 79
    • 0019365718 scopus 로고
    • Peptide synthesis enzymatically catalyzed in a biphasic system: Water-water-immiscible organic solvent
    • Semenov, A. N., Berezin, J. V., and Martinek, K., Peptide synthesis enzymatically catalyzed in a biphasic system: water-water-immiscible organic solvent, Biotechnol. Bioeng.23. 355, 1981.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 355
    • Semenov, A.1    Berezin, N.J.V.2    Martinek, K.3
  • 80
    • 0019879061 scopus 로고
    • Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift
    • Martinek, K., Semenov, A. N„ and Berezin, J. V., Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift, Biochcm. Biophys. Ada,658, 76, 1981.
    • (1981) Biochcm. Biophys. Ada , vol.658 , pp. 76
    • Martinek, K.1    Semenov, A.N.2    Berezin, J.V.3
  • 81
    • 0019879068 scopus 로고
    • Enzymatic synthesis in biphasic aqueous-organic systems. II. Shift of ionic equilibria
    • Martinek, K. and Semenov, A. N., Enzymatic synthesis in biphasic aqueous-organic systems. II. Shift of ionic equilibria, Biocltim. Acta.658, 90, 1981.
    • (1981) Biocltim. Acta , vol.658 , pp. 90
    • Martinek, K.1    Semenov, A.N.2
  • 82
    • 0019761469 scopus 로고
    • Semisynthetic peptides and proteins
    • Chaiken, J. M., Semisynthetic peptides and proteins, Crit. Rev. Biochem., 11, 255, 1981.
    • (1981) Crit. Rev. Biochem. , vol.11 , pp. 255
    • Chaiken, J.M.1
  • 83
    • 1542628195 scopus 로고
    • Peptide bond formation
    • Borsook, H., Peptide bond formation. Adv. Prot. Chem., 8, 127, 1953.
    • (1953) Adv. Prot. Chem. , vol.8 , pp. 127
    • Borsook, H.1
  • 84
    • 0018379810 scopus 로고
    • Energetics of peptide bond formation at elevated temperatures
    • Flegmann, A. W. and Tattersall, R., Energetics of peptide bond formation at elevated temperatures. J. Mol. EvoL.12, 349, 1978.
    • (1978) J. Mol. Evol , vol.12 , pp. 349
    • Flegmann, A.W.1    Tattersall, R.2
  • 85
    • 0020476977 scopus 로고
    • Enzyme peptide synthesis and semisynthesis: Kinetic and thermodynamic aspects
    • Petkov, D. D., Enzyme peptide synthesis and semisynthesis: Kinetic and thermodynamic aspects., J. Theor. Biol.98, 419, 1982.
    • (1982) J. Theor. Biol. , vol.98 , pp. 419
    • Petkov, D.D.1
  • 86
    • 0015932718 scopus 로고
    • Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. A stereochemical interpretation
    • Fersht, A. R., Blow, D. M., and Fastrez, J., Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. A stereochemical interpretation. Biochemistry. 12. 2035. 1973.
    • (1973) Biochemistry , vol.12 , pp. 2035
    • Fersht, A.R.1    Blow, D.M.2    Fastrez, J.3
  • 87
    • 0021761374 scopus 로고
    • Nucleophile specificity in chymotrypsin peptide synthesis
    • Petkov, D. D. and Stoincva, I. B., Nucleophile specificity in chymotrypsin peptide synthesis. Biochem. Biophys. Res. Common., 118, 317, 1984.
    • (1984) Biochem. Biophys. Res. Common. , vol.118 , pp. 317
    • Petkov, D.D.1    Stoincva, I.B.2
  • 88
    • 0001073025 scopus 로고
    • Die Partitionskonstante als Effiz.Ienzparanieter von Nucleophilen bei enzymkatalysierten kinetisch kontrollierten Peptidsynthesen
    • Konnecke, A., Schellenberger, V., Hofmann, H.-J., and Jakubke, H.-D., Die Partitionskonstante als Effiz.ienzparanieter von Nucleophilen bei enzymkatalysierten kinetisch kontrollierten Peptidsynthesen. Pharmazie,39. 785, 1984.
    • (1984) Pharmazie , vol.39 , pp. 785
    • Konnecke, A.1    Schellenberger, V.2    Hofmann, H.-J.3    Jakubke, H.-D.4
  • 90
    • 0001349638 scopus 로고
    • Molecular mechanisms of the ribosomal pepti-dyltransferase center
    • Nierhaus, K. H., Schulze, H., and Cooperman, B. S., Molecular mechanisms of the ribosomal pepti-dyltransferase center, Biochem. Int.1. 185, 1980.
    • (1980) Biochem. Int. , vol.1 , pp. 185
    • Nierhaus, K.H.1    Schulze, H.2    Cooperman, B.S.3
  • 92
    • 33847799412 scopus 로고
    • Structure and mechanisms of chymotrypsin
    • Blow, D. M., Structure and mechanisms of chymotrypsin, Acc. Chem. Res., 9. 145, 1976.
    • (1976) Acc. Chem. Res. , vol.9 , pp. 145
    • Blow, D.M.1
  • 93
    • 84981565026 scopus 로고
    • Proteolytic enzymes. General features of their mode of action
    • Drenth, J., Proteolytic enzymes. General features of their mode of action. Reel. Trav. Chim. Pays-Bas, 99, 185, 1980.
    • (1980) Reel. Trav. Chim. Pays-Bas , vol.99 , pp. 185
    • Drenth, J.1
  • 94
    • 0015209453 scopus 로고
    • Attempts to map a process evolution of peptide biosynthesis
    • Lipmann, F., Attempts to map a process evolution of peptide biosynthesis. Science.173, 875, 1971.
    • (1971) Science , vol.173 , pp. 875
    • Lipmann, F.1
  • 97
    • 85004754595 scopus 로고
    • Side-reactions in peptide synthesis
    • Bodanszky, M. and Martinek, J., Side-reactions in peptide synthesis, Synthesis,333, 1981.
    • (1981) Synthesis , pp. 333
    • Bodanszky, M.1    Martinek, J.2
  • 98
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 99
    • 0003511271 scopus 로고
    • The peptide bond
    • Gross, E. and Meienhofer, J., Eds., Academic Press, New York
    • Gross, E. and Meienhofer, J., The peptide bond, in The Peptides: Analysis, Synthesis, Biology, Vol. 1, Gross, E. and Meienhofer, J., Eds., Academic Press, New York, 1979, 1.
    • (1979) The Peptides: Analysis, Synthesis, Biology , vol.1 , pp. 1
    • Gross, E.1    Meienhofer, J.2
  • 100
    • 0001587747 scopus 로고
    • Racemization in peptide synthesis
    • Gross, E. and Meienhofer, J., Eds., Academic Press, New York
    • Kemp, D. S., Racemization in peptide synthesis, in The Peptides: Analysis, Synthesis, Biology, Vol. 1, Gross, E. and Meienhofer, J., Eds., Academic Press, New York, 1979, 315.
    • (1979) The Peptides: Analysis, Synthesis, Biology , vol.1 , pp. 315
    • Kemp, D.S.1
  • 101
    • 84912680635 scopus 로고
    • Racemisierung der vorletzten carboxylendständigen Aminosäure bei Peptidsynthesen
    • Weygand, F., Prox, A., and König, W., Racemisierung der vorletzten carboxylendständigen Aminosäure bei Peptidsynthesen, Chem. Ber., 99, 1446, 1966.
    • (1966) Chem. Ber. , vol.99 , pp. 1446
    • Weygand, F.1    Prox, A.2    König, W.3
  • 102
    • 84987537697 scopus 로고
    • Racemization of amino acid residue penultimate to C-terminal amino acid
    • Dzieduszyka, M., Smulkowsky, M., and Taszner, E., Racemization of amino acid residue penultimate to C-terminal amino acid, Pol. J. Chem., 53, 1095, 1979.
    • (1979) Pol. J. Chem. , vol.53 , pp. 1095
    • Dzieduszyka, M.1    Smulkowsky, M.2    Taszner, E.3
  • 103
    • 85054419504 scopus 로고
    • Enzyme mechanisms, Enzyme cofactors
    • 3rd ed., Longman Group, London
    • Dixon, M. and Webb, E., Enzyme mechanisms, Enzyme cofactors, in Enzymes, 3rd ed., Longman Group, London, 320, 508, 1979.
    • (1979) Enzymes , vol.320 , pp. 508
    • Dixon, M.1    Webb, E.2
  • 105
    • 0001858739 scopus 로고
    • Enzymes in organic synthesis: Physicochemical means of increasing the yields of end product in biocatalysis
    • Martinek, K. and Semenov, A. N., Enzymes in organic synthesis: physicochemical means of increasing the yields of end product in biocatalysis, J. Appl. Biochem., 3, 93, 1981.
    • (1981) J. Appl. Biochem. , vol.3 , pp. 93
    • Martinek, K.1    Semenov, A.N.2
  • 107
    • 0009402772 scopus 로고
    • The synthesis of peptides
    • Fruton, J. S., The synthesis of peptides, Adv. Prot. Chem., 5, 1, 1949.
    • (1949) Adv. Prot. Chem. , vol.5 , pp. 1
    • Fruton, J.S.1
  • 108
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 109
    • 0001726635 scopus 로고
    • On proteolytic enzymes, XIII. Synthetic substrates for Chymotrypsin
    • Bergmann, M. and Fruton, J. S., On proteolytic enzymes, XIII. Synthetic substrates for Chymotrypsin, J. Biol. Chem., 118, 405, 1937.
    • (1937) J. Biol. Chem. , vol.118 , pp. 405
    • Bergmann, M.1    Fruton, J.S.2
  • 110
    • 0343889591 scopus 로고
    • Some synthetic and hydrolytic experiments with Chymotrypsin
    • Bergmann, M. and Fruton, J. S., Some synthetic and hydrolytic experiments with Chymotrypsin, J. Biol. Chem., 124, 321, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 321
    • Bergmann, M.1    Fruton, J.S.2
  • 111
    • 0006448558 scopus 로고
    • Action of proteolytic enzymes on some peptides and derivatives containing histidine
    • Davis, N. C., Action of proteolytic enzymes on some peptides and derivatives containing histidine, J. Biol. Chem., 223, 935, 1956.
    • (1956) J. Biol. Chem. , vol.223 , pp. 935
    • Davis, N.C.1
  • 112
    • 84914296904 scopus 로고
    • Structural requirements of specific substrates for Chymotrypsin. II. An analysis of the contribution of the structural components to enzymatic hydrolysis
    • Kaufman, S. and Neurath, H., Structural requirements of specific substrates for Chymotrypsin. II. An analysis of the contribution of the structural components to enzymatic hydrolysis, Arch. Biochem. Biophys., 21, 437, 1949.
    • (1949) Arch. Biochem. Biophys. , vol.21 , pp. 437
    • Kaufman, S.1    Neurath, H.2
  • 114
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. and Berger, A., On the size of the active site in proteases. I. Papain, Biochem. Biophys. Res. Commun., 27, 157, 1967.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157
    • Schechter, I.1    Berger, A.2
  • 115
    • 78651155158 scopus 로고
    • Über enzymatische Verseifung von Peptid-Estern, Hoppe-Seyler's Z
    • Kloss, G. and Schroder, E., Über enzymatische Verseifung von Peptid-Estern, Hoppe-Seyler's Z. Physiol. Chem., 336, 248, 1964.
    • (1964) Physiol. Chem. , vol.336 , pp. 248
    • Kloss, G.1    Schroder, E.2
  • 116
    • 0017805504 scopus 로고
    • Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and a-chymotrypsin: Enzyme-substrate interactions
    • Bauer, C.-A., Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and a-chymotrypsin: enzyme-substrate interactions, Biochemistry,17, 375, 1978.
    • (1978) Biochemistry , vol.17 , pp. 375
    • Bauer, C.-A.1
  • 117
    • 0017379736 scopus 로고
    • A-Chymotrypsin as the catalyst for peptide synthesis
    • Morihara, K. and Oka, T., a-Chymotrypsin as the catalyst for peptide synthesis, Biochem. J., 163, 531, 1977.
    • (1977) Biochem. J. , vol.163 , pp. 531
    • Morihara, K.1    Oka, T.2
  • 118
    • 0000463537 scopus 로고
    • The correlation of the pH (PD) dependence and the stepwise mechanism of a-chymotrypsin-catalyzed reactions
    • Bender, M. L., Clement, G. E., Kezdy, F. J., and Heck, H. D. A., The correlation of the pH (pD) dependence and the stepwise mechanism of a-chymotrypsin-catalyzed reactions, J. Am. Chem. Soc., 86, 3680, 1964.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 3680
    • Bender, M.L.1    Clement, G.E.2    Kezdy, F.J.3    Heck, H.4
  • 119
    • 0015932715 scopus 로고
    • Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by Chymotrypsin
    • Fastrez, J. and Fersht, A. R., Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by Chymotrypsin, Biochemistry,12, 2025, 1973.
    • (1973) Biochemistry , vol.12 , pp. 2025
    • Fastrez, J.1    Fersht, A.R.2
  • 120
    • 0014694662 scopus 로고
    • Comparison of a-chymotrypsin and subtilisin BPN': Size and specificity of the active site
    • Morihara, K., Oka, T., and Tsuzuki, H., Comparison of a-chymotrypsin and subtilisin BPN': size and specificity of the active site, Biochem. Biophys. Res. Commun., 35, 210, 1969.
    • (1969) Biochem. Biophys. Res. Commun. , vol.35 , pp. 210
    • Morihara, K.1    Oka, T.2    Tsuzuki, H.3
  • 121
    • 0017603204 scopus 로고
    • A kinetic investigation of subsites S, and S2 in a-chymotrypsin and subtilisin BPN
    • 2 in a-chymotrypsin and subtilisin BPN', Arch. Biochem. Biophys., 178, 188, 1977.
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 188
    • Morihara, K.1    Oka, T.2
  • 123
    • 0018038885 scopus 로고
    • Peptide bond synthesis catalyzed by a-chymotrypsin
    • Oka, T. and Morihara, M., Peptide bond synthesis catalyzed by a-chymotrypsin, J. Biochem. (Tokyo), 84, 1277, 1978.
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 1277
    • Oka, T.1    Morihara, M.2
  • 124
    • 0017599322 scopus 로고
    • Co-oligopeptides of aromatic amino acids and glycine with variable distance between the aromatic residues. VII. Enzymatic synthesis of A-protected peptide amides
    • Saltman, R., Vlach, D., and Luisi, P. L., Co-oligopeptides of aromatic amino acids and glycine with variable distance between the aromatic residues. VII. Enzymatic synthesis of A-protected peptide amides, Biopolymers,16, 631, 1977.
    • (1977) Biopolymers , vol.16 , pp. 631
    • Saltman, R.1    Vlach, D.2    Luisi, P.L.3
  • 125
    • 0017576079 scopus 로고
    • Co-oligopeptides of glycine and aromatic amino acids with variable distance between the aromatic residues. VIII. Enzymatic synthesis of A'-protected dipeptide esters
    • Luisi, P. L., Saltman, R., Vlach, D., and Guarnaccia, R., Co-oligopeptides of glycine and aromatic amino acids with variable distance between the aromatic residues. VIII. Enzymatic synthesis of A'-protected dipeptide esters, J. Mol. Catalysis,2, 133, 1977.
    • (1977) J. Mol. Catalysis , vol.2 , pp. 133
    • Luisi, P.L.1    Saltman, R.2    Vlach, D.3    Guarnaccia, R.4
  • 126
    • 0013554686 scopus 로고
    • The primary specificity of a-chymotrypsin. Acylated amino acid esters with normal alkyl side chains
    • Jones, J. B., Kunitake, T., Niemann, C., and Hein, G. E., The primary specificity of a-chymotrypsin. Acylated amino acid esters with normal alkyl side chains, J. Am. Chem. Soc., 87, 1777, 1965.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 1777
    • Jones, J.B.1    Kunitake, T.2    Niemann, C.3    Hein, G.E.4
  • 127
    • 29344442136 scopus 로고
    • Serine-protease-assisted synthesis of peptide substrates for a-chymotrypsin
    • Bizzozero, S. A., Rovagnati, B. A., and Dutler, H., Serine-protease-assisted synthesis of peptide substrates for a-chymotrypsin, Helv. Chim. Acta, 65,1707, 1982.
    • (1982) Helv. Chim. Acta , vol.65 , pp. 1707
    • Bizzozero, S.A.1    Rovagnati, B.A.2    Dutler, H.3
  • 128
    • 0012594845 scopus 로고
    • Enzyme-catalyzed peptide bond formation: Elastase- and 8-chymotrypsin-assisted synthesis of oligopeptides
    • Bizzozero, S. A., Dutler, H., Franzstack, R., and Rovagnati, B. A., Enzyme-catalyzed peptide bond formation: elastase- and 8-chymotrypsin-assisted synthesis of oligopeptides, Helv. Chim. Acta,68, 981, 1985.
    • (1985) Helv. Chim. Acta , vol.68 , pp. 981
    • Bizzozero, S.A.1    Dutler, H.2    Franzstack, R.3    Rovagnati, B.A.4
  • 129
  • 131
    • 77956714255 scopus 로고
    • The properties of proteins in nonaqueous solvents
    • Singer, S. J., The properties of proteins in nonaqueous solvents, Adv. Prot. Chem., 17, 1, 1962.
    • (1962) Adv. Prot. Chem. , vol.17 , pp. 1
    • Singer, S.J.1
  • 132
    • 0018278636 scopus 로고
    • Synthesis of peptide bonds by proteinases. Addition of cosolvents shifts peptide bond equilibria toward synthesis
    • Homandberg, G. A., Mattis, J. A., and Laskowksi, M., Jr., Synthesis of peptide bonds by proteinases. Addition of cosolvents shifts peptide bond equilibria toward synthesis, Biochemistry,17, 5220, 1978.
    • (1978) Biochemistry , pp. 5220
    • Homandberg, G.A.1    Mattis, J.A.2    Laskowksi, M.3
  • 134
    • 0019365718 scopus 로고
    • Peptide synthesis enzymatically catalyzed in a biphasic system: Water - water immiscible organic solvent
    • Semenov, A. N., Berezin, I. V., and Martinek, K., Peptide synthesis enzymatically catalyzed in a biphasic system: water - water immiscible organic solvent, Biotechnol. Bioeng., 23, 355, 1981.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 355
    • Semenov, A.N.1    Berezin, I.V.2    Martinek, K.3
  • 135
    • 0019879068 scopus 로고
    • Enzymatic synthesis in biphasic aqueous-organic systems. II. Shift of ionic equilibria
    • Martinek, K. and Semenov, A. N., Enzymatic synthesis in biphasic aqueous-organic systems. II. Shift of ionic equilibria, Biochim. Biophys. Acta,658, 90, 1981.
    • (1981) Biochim. Biophys. Acta , vol.658 , pp. 90
    • Martinek, K.1    Semenov, A.N.2
  • 136
    • 0012245852 scopus 로고
    • Enzyme-catalyzed peptide synthesis in a two-phase aqueous-organic system
    • Martinek, K., Semenov, A. N., and Berezin, I. V., Enzyme-catalyzed peptide synthesis in a two-phase aqueous-organic system, Dokl. Akad. Nauk. SSSR,254, 121, 1980.
    • (1980) Dokl. Akad. Nauk. SSSR , vol.254 , pp. 121
    • Martinek, K.1    Semenov, A.N.2    Berezin, I.V.3
  • 137
    • 0342639673 scopus 로고
    • A-Chymotrypsinkatalysierte Synthese von Tripeptidamiden im wässrig-organischen Zweiphasensystem
    • Kuhl, P., Posselt, S., and Jakubke, H.-D., a-Chymotrypsinkatalysierte Synthese von Tripeptidamiden im wässrig-organischen Zweiphasensystem, Pharmazie,36, 463, 1981.
    • (1981) Pharmazie , vol.36 , pp. 463
    • Kuhl, P.1    Posselt, S.2    Jakubke, H.3
  • 138
    • 0012556887 scopus 로고
    • Peptide synthesis by means of immobilized enzymes. I. Immobilized a-chymotrypsin
    • Könnecke, A., Bullerjahn, R., and Jakubke, H.-D., Peptide synthesis by means of immobilized enzymes. I. Immobilized a-chymotrypsin, Monatsh. Chem., 112, 469, 1981.
    • (1981) Monatsh. Chem. , vol.112 , pp. 469
    • Könnecke, A.1    Bullerjahn, R.2    Jakubke, H.-D.3
  • 139
    • 84913714366 scopus 로고
    • Untersuchungen zum Einfluss der Reaktionsbedingungen auf die a-chymotrypsinkatalysierte Peptidsynthese im wässrig-organischen Zweiphasensystem
    • Kuhl, P., Walpuski, J., and Jakubke, H.-D., Untersuchungen zum Einfluss der Reaktionsbedingungen auf die a-chymotrypsinkatalysierte Peptidsynthese im wässrig-organischen Zweiphasensystem, Pharmazie, 37, 766, 1982.
    • (1982) Pharmazie , vol.37 , pp. 766
    • Kuhl, P.1    Walpuski, J.2    Jakubke, H.-D.3
  • 140
    • 4243425565 scopus 로고
    • Model studies on the utility of nucleophiles bound to insoluble supports for enzymatic peptide synthesis
    • Könnecke, A., Dettlaff, S., and Jakubke, H.-D., Model studies on the utility of nucleophiles bound to insoluble supports for enzymatic peptide synthesis, Monatsh. Chem., 113, 331, 1982.
    • (1982) Monatsh. Chem. , vol.113 , pp. 331
    • Könnecke, A.1    Dettlaff, S.2    Jakubke, H.-D.3
  • 141
    • 84914396421 scopus 로고
    • Proteasekatalysierte (2 + 2)-Segmentkondensation im wässrigorganischen Zweiphasensystem
    • Kuhl, P., Döring, G., and Jakubke, H.-D., Proteasekatalysierte (2 + 2)-Segmentkondensation im wässrigorganischen Zweiphasensystem, Pharmazie,38, 371, 1983.
    • (1983) Pharmazie , vol.38 , pp. 371
    • Kuhl, P.1    Döring, G.2    Jakubke, H.3
  • 142
    • 0000826402 scopus 로고
    • Enzymatic synthesis of hydrocarbon-soluble peptides with reverse micelles
    • Liithi, P. and Luisi, P. L., Enzymatic synthesis of hydrocarbon-soluble peptides with reverse micelles, J. Am. Chem. Soc., 106, 7285, 1984.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7285
    • Liithi, P.1    Luisi, P.L.2
  • 143
    • 0019964097 scopus 로고
    • Proteasen als Biokatalysatoren für die Peptidsynthese
    • Jakubke, H.-D. and Kuhl, P., Proteasen als Biokatalysatoren für die Peptidsynthese, Pharmazie,37, 89, 1982.
    • (1982) Pharmazie , vol.37 , pp. 89
    • Jakubke, H.-D.1    Kuhl, P.2
  • 144
    • 0344520082 scopus 로고
    • Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung
    • Jakubke, H.-D., Kuhl, P., and Könnecke, A., Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung, Angew. Chem., 97, 79, 1985.
    • (1985) Angew. Chem. , vol.97 , pp. 79
    • Jakubke, H.-D.1    Kuhl, P.2    Könnecke, A.3
  • 145
    • 0021269160 scopus 로고
    • A-Chymotrypsinkatalysierte Peptidsynthesen unter Verwendung des 4-Sulfobenzylrestes als solubisierende Carboxylschutzgruppe
    • Kuhl, P., Walpuski, J., and Jakubke, H.-D., a-Chymotrypsinkatalysierte Peptidsynthesen unter Verwendung des 4-Sulfobenzylrestes als solubisierende Carboxylschutzgruppe, Pharmazie,39, 280, 1984.
    • (1984) Pharmazie , vol.39 , pp. 280
    • Kuhl, P.1    Walpuski, J.2    Jakubke, H.-D.3
  • 146
    • 85054400158 scopus 로고
    • Der 2-Thiosulfatoethylrest als solubisierende Schutzgruppe in der enzymatischen Peptidsynthese
    • Kuhl, P., Walpuski, J., and Jakubke, H.-D., Der 2-Thiosulfatoethylrest als solubisierende Schutzgruppe in der enzymatischen Peptidsynthese, Pharmazie,40, 465, 1985.
    • (1985) Pharmazie , vol.40 , pp. 465
    • Kuhl, P.1    Walpuski, J.2    Jakubke, H.-D.3
  • 147
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • Merrifield, R. B., Solid phase peptide synthesis. I. The synthesis of a tetrapeptide, J. Am. Chem. Soc., 85, 2149, 1963.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149
    • Merrifield, R.B.1
  • 148
    • 34250117428 scopus 로고
    • Solubisierende Schutzgruppen für enzymatische Peptidsynthesen. Untersuchungen mit Polyoxyethylen-gebundenen Substraten
    • Könnecke, A., Pchalek, V., and Jakubke, H.-D., Solubisierende Schutzgruppen für enzymatische Peptidsynthesen. Untersuchungen mit Polyoxyethylen-gebundenen Substraten, Monatsh. Chem., 116, 111, 1985.
    • (1985) Monatsh. Chem. , vol.116 , pp. 111
    • Könnecke, A.1    Pchalek, V.2    Jakubke, H.-D.3
  • 149
    • 0001120111 scopus 로고
    • Eine neue Methode zur Synthese von Polypeptiden
    • Mutter, M., Hagenmaier, H., and Bayer, E., Eine neue Methode zur Synthese von Polypeptiden, Angew. Chem., 83, 883, 1971.
    • (1971) Angew. Chem. , vol.83 , pp. 883
    • Mutter, M.1    Hagenmaier, H.2    Bayer, E.3
  • 150
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber, R. and Bode, W., Structural basis of the activation and action of trypsin, Acc. Chem. Res., 11, 114, 1978.
    • (1978) Acc. Chem. Res. , vol.11 , pp. 114
    • Huber, R.1    Bode, W.2
  • 151
    • 0000119209 scopus 로고
    • Trypsinogen and chymotrypsinogen as homologous proteins
    • Walsh, K. A. and Neurath, H., Trypsinogen and chymotrypsinogen as homologous proteins, Proc. Natl. Acad. Sei. U.S.A., 52, 884, 1964.
    • (1964) Proc. Natl. Acad. Sei. U.S.A. , vol.52 , pp. 884
    • Walsh, K.A.1    Neurath, H.2
  • 152
    • 76549208435 scopus 로고
    • The chemistry and structure of peptides and proteins
    • Keil, B., The chemistry and structure of peptides and proteins, Ann. Rev. Biochem., 34, 175, 1965.
    • (1965) Ann. Rev. Biochem. , vol.34 , pp. 175
    • Keil, B.1
  • 153
    • 77956910473 scopus 로고
    • Trypsin
    • 3rd Ed., Part III, Boyer, P. D., Ed., Academic Press, New York
    • Keil, B., Trypsin, in The Enzymes, 3rd Ed., Part III, Boyer, P. D., Ed., Academic Press, New York, 1971, 249.
    • (1971) The Enzymes , pp. 249
    • Keil, B.1
  • 154
    • 0017729536 scopus 로고
    • Trypsin as a catalyst for peptide synthesis
    • Oka, T. and Morihara, K., Trypsin as a catalyst for peptide synthesis, J. Biochem. (Tokyo),82, 1055, 1977.
    • (1977) J. Biochem. (Tokyo) , vol.82 , pp. 1055
    • Oka, T.1    Morihara, K.2
  • 155
    • 0019058231 scopus 로고
    • Coupling between Cbz-Arg-OH and Leu-X catalyzed by trypsin and papain
    • Tsuzuki, H., Oka, T., and Morihara, K., Coupling between Cbz-Arg-OH and Leu-X catalyzed by trypsin and papain, J. Biochem. (Tokyo),88, 669, 1980.
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 669
    • Tsuzuki, H.1    Oka, T.2    Morihara, K.3
  • 158
    • 0012500370 scopus 로고
    • Peptidsynthesen mit immobilisierten Enzymen. II. Immobilisiertes Trypsin, Thermolysin und Papain
    • Konnecke, A., Hansler, M., Schellenberger, V., and Jakubke, H.-D., Peptidsynthesen mit immobilisierten Enzymen. II. Immobilisiertes Trypsin, Thermolysin und Papain, Monatsh. Chem., 114, 433, 1983.
    • (1983) Monatsh. Chem. , vol.114 , pp. 433
    • Konnecke, A.1    Hansler, M.2    Schellenberger, V.3    Jakubke, H.-D.4
  • 159
    • 0016376184 scopus 로고
    • Comparitive specificity of microbial proteinases
    • Morihara, K., Comparitive specificity of microbial proteinases, Adv. Enzymol. Relat. Areas Mol. Biol., 41, 179, 1974.
    • (1974) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.41 , pp. 179
    • Morihara, K.1
  • 160
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut, J., Serine proteases: structure and mechanism of catalysis, Ann. Rev. Biochem., 46, 331, 1977.
    • (1977) Ann. Rev. Biochem. , vol.46 , pp. 331
    • Kraut, J.1
  • 161
    • 33847799412 scopus 로고
    • Structure and mechanism of chymotrypsin
    • Blow, D. M., Structure and mechanism of chymotrypsin, Acc. Chem. Res., 9, 145, 1976.
    • (1976) Acc. Chem. Res. , vol.9 , pp. 145
    • Blow, D.M.1
  • 163
    • 0001569784 scopus 로고
    • The enzymatic synthesis of protected valine-5 angiotensin amide-1
    • Isowa, Y., Ohmori, M., Sato, M., and Mori, K., The enzymatic synthesis of protected valine-5 angiotensin amide-1, Bull. Chem. Soc. Jpn., 50, 2766, 1977.
    • (1977) Bull. Chem. Soc. Jpn. , vol.50 , pp. 2766
    • Isowa, Y.1    Ohmori, M.2    Sato, M.3    Mori, K.4
  • 164
    • 0019531434 scopus 로고
    • Peptide bond synthesis catalyzed by subtilisin, papain, and pepsin
    • Morihara, K. and Oka, T., Peptide bond synthesis catalyzed by subtilisin, papain, and pepsin, J. Biochem. (Tokyo),89, 385, 1981.
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 385
    • Morihara, K.1    Oka, T.2
  • 165
    • 0000065905 scopus 로고
    • Peptide synthesis catalyzed by serine proteinases. Acylpeptide esters as carboxyl components (in Russian)
    • Voyushina, T. L., Lyublinskaya, L. A., and Stepanov, V. M., Peptide synthesis catalyzed by serine proteinases. Acylpeptide esters as carboxyl components (in Russian), Bioorg. Khim., 11, 738, 1985.
    • (1985) Bioorg. Khim. , vol.11 , pp. 738
    • Voyushina, T.L.1    Lyublinskaya, L.A.2    Stepanov, V.M.3
  • 166
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 167
    • 0014747224 scopus 로고
    • Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester: A new highly specific elastase substrate
    • Gertler, A. and Hofman, T., Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester: a new highly specific elastase substrate, Can. J. Biochem., 48, 384, 1970.
    • (1970) Can. J. Biochem. , vol.48 , pp. 384
    • Gertler, A.1    Hofman, T.2
  • 168
    • 0015911769 scopus 로고
    • Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates
    • Thompson, R. C. and Blout, E. R., Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates, Biochemistry,12, 57, 1973.
    • (1973) Biochemistry , vol.12 , pp. 57
    • Thompson, R.C.1    Blout, E.R.2
  • 169
    • 34250236496 scopus 로고
    • Versuche zur Anwendung von Thermitase als Katalysator zur Kniip-fung der Peptidbindung
    • Konnecke, A. and Jakubke, H.-D., Versuche zur Anwendung von Thermitase als Katalysator zur Kniip-fung der Peptidbindung, Monatsh. Chem., 112, 1099, 1981.
    • (1981) Monatsh. Chem. , vol.112 , pp. 1099
    • Konnecke, A.1    Jakubke, H.-D.2
  • 170
    • 0017270022 scopus 로고
    • Carboxypeptidase Y
    • Hayashi, R., Carboxypeptidase Y, Methods Enzymol., 45, 568, 1976.
    • (1976) Methods Enzymol. , vol.45 , pp. 568
    • Hayashi, R.1
  • 171
    • 0001927074 scopus 로고
    • Enzymatic peptide synthesis. Carboxypeptidase Y catalyzed formation of peptide bonds
    • Widmer, F. and Johansen, J. T., Enzymatic peptide synthesis. Carboxypeptidase Y catalyzed formation of peptide bonds, Carlsberg Res. Commun., 44, 37, 1979.
    • (1979) Carlsberg Res. Commun. , vol.44 , pp. 37
    • Widmer, F.1    Johansen, J.T.2
  • 172
    • 0016659095 scopus 로고
    • Kinetic studies of carboxypeptidase Y. I. Kinetic parameters for the hydrolysis of synthetic substrates
    • Hayashi, R., Bai, Y., and Hata, T., Kinetic studies of carboxypeptidase Y. I. Kinetic parameters for the hydrolysis of synthetic substrates, J. Biochem. (Tokyo),77, 69, 1975.
    • (1975) J. Biochem. (Tokyo) , vol.77 , pp. 69
    • Hayashi, R.1    Bai, Y.2    Hata, T.3
  • 173
    • 0001831662 scopus 로고
    • Influence of the structure of amine components on carboxypeptidase Y catalyzed amide bond formation
    • Widmer, F., Breddam, K., and Johansen, J. T., Influence of the structure of amine components on carboxypeptidase Y catalyzed amide bond formation, Carlsberg Res. Commun., 46, 97, 1981.
    • (1981) Carlsberg Res. Commun. , vol.46 , pp. 97
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 174
    • 0000990957 scopus 로고
    • Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components, Carlsberg Res. Commun., 45, 453, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 453
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 175
    • 0012606494 scopus 로고
    • Amino acid methyl esters as amine components in CPD-Y catalyzed peptide synthesis: Control of side reactions
    • Breddam, K., Widmer, F., and Johansen, J. T., Amino acid methyl esters as amine components in CPD-Y catalyzed peptide synthesis: control of side reactions, Carlsberg Res. Commun., 48, 231, 1983.
    • (1983) Carlsberg Res. Commun. , vol.48 , pp. 231
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 176
    • 0011300588 scopus 로고
    • Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis
    • Breddam, K., Widmer, F., and Johansen, J. T., Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis, Carlsberg Res. Commun., 45, 237, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 237
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 177
    • 34250153616 scopus 로고
    • Model studies on carboxypeptidase Y catalyzed peptide synthesis in an aqueous-organic two-phase system
    • Kuhl, P., Zapevalova, N. P., Konnecke, A., and Jakubke, H.-D., Model studies on carboxypeptidase Y catalyzed peptide synthesis in an aqueous-organic two-phase system, Monatsh. Chem., 114, 343, 1983.
    • (1983) Monatsh. Chem. , vol.114 , pp. 343
    • Kuhl, P.1    Zapevalova, N.P.2    Konnecke, A.3    Jakubke, H.-D.4
  • 178
    • 0002918033 scopus 로고
    • The enzymatic synthesis of peptide bonds
    • Bergmann, M. and Fraenkel-Conrat, H., The enzymatic synthesis of peptide bonds, J. Biol. Chem., 124, 1, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 1
    • Bergmann, M.1    Fraenkel-Conrat, H.2
  • 179
    • 0009349295 scopus 로고
    • On proteolytic enzymes. VI. On the specificity of papain
    • Bergmann, M., Zervas, L., and Fruton, J. S., On proteolytic enzymes. VI. On the specificity of papain, J. Biol. Chem., Ill, 225, 1935.
    • (1935) J. Biol. Chem., Ill , pp. 225
    • Bergmann, M.1    Zervas, L.2    Fruton, J.S.3
  • 180
    • 62949129211 scopus 로고
    • Specificity of papain-catalyzed transamidation reactions
    • Mycek, M. J. and Fruton, J. S., Specificity of papain-catalyzed transamidation reactions, J. Biol. Chem., 226, 165, 1957.
    • (1957) J. Biol. Chem. , vol.226 , pp. 165
    • Mycek, M.J.1    Fruton, J.S.2
  • 181
  • 182
    • 2142822422 scopus 로고
    • The oxidative cleavage of phenylhydrazide groups from carboallyloxy-a-amino acid phenylhydrazides and carboallyloxydipeptide phenylhydrazides
    • Milne, H. B., Halver, J. E., Ho, D. S., and Mason, M. S., The oxidative cleavage of phenylhydrazide groups from carboallyloxy-a-amino acid phenylhydrazides and carboallyloxydipeptide phenylhydrazides, J. Am. Chem. Soc., 79, 637, 1957.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 637
    • Milne, H.B.1    Halver, J.2    Ho, E.D.S.3    Mason, M.S.4
  • 184
    • 76549233424 scopus 로고
    • Enzymic synthesis of peptide bonds. II. Preferences of papain within the monoaminomonocarboxylic acid series
    • Fox, S. W., Pettinga, C. W., Halverson, J. S., and Wax, H., Enzymic synthesis of peptide bonds. II. Preferences of papain within the monoaminomonocarboxylic acid series, Arch. Biochem., 25, 13, 1950.
    • (1950) Arch. Biochem. , vol.25 , pp. 13
    • Fox, S.W.1    Pettinga, C.W.2    Halverson, J.S.3    Wax, H.4
  • 185
    • 76549233424 scopus 로고
    • Enzymic synthesis of peptide bonds. I. Some factors which influence the synthesis of peptide bond as catalyzed by papain
    • Fox, S. W. and Pettinga, C. W., Enzymic synthesis of peptide bonds. I. Some factors which influence the synthesis of peptide bond as catalyzed by papain, Arch. Biochem., 25, 13, 1950.
    • (1950) Arch. Biochem. , vol.25 , pp. 13
    • Fox, S.W.1    Pettinga, C.W.2
  • 186
    • 15544369959 scopus 로고
    • Enzymatically catalyzed synthesis of dipeptides of "y-carboxyl-i.-glutamic acid from benzyloxycarbonyl-y-carboxy-DL-glutamic acid
    • Cefovsky, V. and JoSt, K., Enzymatically catalyzed synthesis of dipeptides of "y-carboxyl-i.-glutamic acid from benzyloxycarbonyl-y-carboxy-DL-glutamic acid, Coll. Czech. Chem. Commun., 50, 878, 1985.
    • (1985) Coll. Czech. Chem. Commun. , vol.50 , pp. 878
    • Cefovsky, V.1    Jost, K.2
  • 187
  • 188
    • 25044473175 scopus 로고
    • Modelluntersuchungen zur Papainkatalysierten Peptidsynthese im wässrig-organischen Zweiphasensystem
    • Döring, G., Kuhl, P., and Jakubke, H.-D., Modelluntersuchungen zur Papainkatalysierten Peptidsynthese im wässrig-organischen Zweiphasensystem, Monatsh. Chem., 112, 1165, 1981.
    • (1981) Monatsh. Chem. , vol.112 , pp. 1165
    • Döring, G.1    Kuhl, P.2    Jakubke, H.-D.3
  • 189
    • 0001192303 scopus 로고
    • Kinetics of papain-catalyzed hydrolysis of a-A'-Benzyol-L-arginine ethyl ester and a-N-Benzoyl-L-arginineamide
    • Whitaker, J. R. and Bender, M. L., Kinetics of papain-catalyzed hydrolysis of a-A'-Benzyol-L-arginine ethyl ester and a-N-Benzoyl-L-arginineamide, J. Am. Chem. Soc., 87, 2728, 1965.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2728
    • Whitaker, J.R.1    Bender, M.L.2
  • 190
    • 0016914760 scopus 로고
    • The mechanism of the catalytic action of pepsin and related acid proteinases
    • Fruton, J. S., The mechanism of the catalytic action of pepsin and related acid proteinases, Adv. Enzymol. Relat. Areas Mol. Biol., 44, 1, 1976.
    • (1976) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.44 , pp. 1
    • Fruton, J.S.1
  • 191
  • 192
    • 85054359595 scopus 로고
    • The unravelling of biosynthetic pathways
    • Elsevier, Amsterdam
    • Florkin, M. and Stotz, E. H., The unravelling of biosynthetic pathways, in Comprehensive Biochemistry, Vol. 32, Elsevier, Amsterdam, 1977, 307.
    • (1977) Comprehensive Biochemistry , vol.32 , pp. 307
    • Florkin, M.1    Stotz, E.H.2
  • 193
    • 84982059488 scopus 로고
    • Untersuchungen über die Plastein-Reaktion. Isolierung einheitlicher Plastein-Bausteine
    • Wieland, T., Determann, H., and Albrecht, E., Untersuchungen über die Plastein-Reaktion. Isolierung einheitlicher Plastein-Bausteine, Justus Liebigs Ann. Chem., 633, 185, 1960.
    • (1960) Justus Liebigs Ann. Chem. , vol.633 , pp. 185
    • Wieland, T.1    Determann, H.2    Albrecht, E.3
  • 194
    • 84932491596 scopus 로고
    • Pepsin induced synthesis of peptide bonds
    • Goodman, M. and Meienhofer, J., Eds., Wiley and Sons, New York
    • Pellegrini, A. and Luisi, P. L., Pepsin induced synthesis of peptide bonds, in Peptides, Proc. 5th Am. Peptide Symp., Goodman, M. and Meienhofer, J., Eds., Wiley and Sons, New York, 1977, 556.
    • (1977) Peptides, Proc. 5Th Am. Peptide Symp , pp. 556
    • Pellegrini, A.1    Luisi, P.L.2
  • 195
    • 0018094411 scopus 로고
    • Pepsin-catalyzed peptide synthesis
    • Pellegrini, A. and Luisi, P. L., Pepsin-catalyzed peptide synthesis, Biopolymers,17, 2573, 1978.
    • (1978) Biopolymers , vol.17 , pp. 2573
    • Pellegrini, A.1    Luisi, P.L.2
  • 196
    • 49049126388 scopus 로고
    • Enzymic synthesis of oligopeptides. VI. The mechanistic features of pepsin-catalyzed peptide synthesis
    • Tseng, M.-J., Wu, S-H., and Wang, K.-T., Enzymic synthesis of oligopeptides. VI. The mechanistic features of pepsin-catalyzed peptide synthesis, Tetrahedron,39, 61, 1983.
    • (1983) Tetrahedron , vol.39 , pp. 61
    • Tseng, M.-J.1    Wu, S.-H.2    Wang, K.-T.3
  • 197
    • 84990159397 scopus 로고
    • Enzymatic peptide synthesis
    • Isowa, Y., Enzymatic peptide synthesis, Yuki Gasei Kagaku,36, 195, 1987.
    • (1987) Yuki Gasei Kagaku , vol.36 , pp. 195
    • Isowa, Y.1
  • 198
    • 3042967033 scopus 로고
    • Modelluntersuchungen zur pepsinkatalysierten Peptidsynthese im wässrig-organischen Zweiphasensystem
    • Kuhl, P., Wilsdorf, A., and Jakubke, H.-D., Modelluntersuchungen zur pepsinkatalysierten Peptidsynthese im wässrig-organischen Zweiphasensystem, Monatsh. Chem., 114, 571, 1983.
    • (1983) Monatsh. Chem. , vol.114 , pp. 571
    • Kuhl, P.1    Wilsdorf, A.2    Jakubke, H.-D.3
  • 200
    • 0015237801 scopus 로고
    • Studies on the role of calcium in thermolysin
    • Feder, J., Garret, L. R., and Wildi, B. S., Studies on the role of calcium in thermolysin, Biochemistry, 10, 4552, 1971.
    • (1971) Biochemistry , vol.10 , pp. 4552
    • Feder, J.1    Garret, L.R.2    Wildi, B.S.3
  • 201
    • 0014828815 scopus 로고
    • Thermolysin: Kinetic study with oligopeptides
    • Morihara, K. and Tsuzuki, H., Thermolysin: kinetic study with oligopeptides, Eur. J. Biochem., 15, 374, 1970.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 374
    • Morihara, K.1    Tsuzuki, H.2
  • 202
    • 0017395121 scopus 로고
    • Crystallographic study of the binding of dipeptide inhibitors to thermolysin: Implications for the mechanism of catalysis
    • Kester, W. R. and Matthews, B. W., Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis, Biochemistry,16, 2506, 1977.
    • (1977) Biochemistry , vol.16 , pp. 2506
    • Kester, W.R.1    Matthews, B.W.2
  • 203
    • 0018082849 scopus 로고
    • Acyl and amino intermediates in reactions catalyzed by thermolysin
    • Morihara, K., Tsuzuki, H., and Oka, T., Acyl and amino intermediates in reactions catalyzed by thermolysin, Biochem. Biophys. Res. Commun., 84, 95, 1978.
    • (1978) Biochem. Biophys. Res. Commun. , vol.84 , pp. 95
    • Morihara, K.1    Tsuzuki, H.2    Oka, T.3
  • 204
    • 0000816516 scopus 로고
    • Syntheses of A-acyl dipeptide derivatives by metalloproteinases
    • Isowa, Y. and Ichikawa, T., Syntheses of A-acyl dipeptide derivatives by metalloproteinases, Bull. Chem. Soc. Jpn., 52, 796, 1979.
    • (1979) Bull. Chem. Soc. Jpn. , vol.52 , pp. 796
    • Isowa, Y.1    Ichikawa, T.2
  • 205
    • 49249152719 scopus 로고
    • The thermolysin-catalyzed condensation reactions of /V-subslituted aspartic and glutamic acids with phenylalanine alkyl esters
    • Isowa, Y., Ohmori, M., Ichikawa, T., Mori, K., Nonaka, Y., Kihara, K., Oyama, K., Satoh, H., and Nishimura, S., The thermolysin-catalyzed condensation reactions of /V-subslituted aspartic and glutamic acids with phenylalanine alkyl esters, Tetrahedron Lett., 22, 2611, 1979.
    • (1979) Tetrahedron Lett. , vol.22 , pp. 2611
    • Isowa, Y.1    Ohmori, M.2    Ichikawa, T.3    Mori, K.4    Nonaka, Y.5    Kihara, K.6    Oyama, K.7    Satoh, H.8    Nishimura, S.9
  • 206
    • 0019057814 scopus 로고
    • Peptide bond synthesis catalyzed by thermolysin
    • Oka, T. and Morihara, K., Peptide bond synthesis catalyzed by thermolysin, J. Biochem. (Tokyo),88, 807, 1980.
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 807
    • Oka, T.1    Morihara, K.2
  • 207
    • 84932456195 scopus 로고
    • Thermolysin-katalysierte Peptidsynthese im wässrig-organischen Zwei-phasen-system
    • Kuhl, P. and Jakubke, H.-D., Thermolysin-katalysierte Peptidsynthese im wässrig-organischen Zwei-phasen-system, Z. Chem., 22, 407, 1982.
    • (1982) Z. Chem , vol.22 , pp. 407
    • Kuhl, P.1    Jakubke, H.-D.2
  • 208
    • 33845558341 scopus 로고
    • Synthesis of an aspartame precursor by immobilized thermolysin in an organic solvent
    • Oyama, K., Nishimura, S., Nonaka, Y., Kihara, K., and Hashimoto, T., Synthesis of an aspartame precursor by immobilized thermolysin in an organic solvent, J. Org. Chem., 46, 5241, 1981.
    • (1981) J. Org. Chem. , vol.46 , pp. 5241
    • Oyama, K.1    Nishimura, S.2    Nonaka, Y.3    Kihara, K.4    Hashimoto, T.5
  • 209
    • 0021848865 scopus 로고
    • Continous synthesis of: V-(Benzyloxycarbonyl)-l-aspartyl-L-phenylalanine methyl ester with immobilized thermolysin in an organic solvent
    • Nakanishi, K., Kamikubo, T., and Matsuno, R., Continous synthesis of:V-(Benzyloxycarbonyl)-l-aspartyl-L-phenylalanine methyl ester with immobilized thermolysin in an organic solvent, Biotechnology, 3, 459, 1985.
    • (1985) Biotechnology , vol.3 , pp. 459
    • Nakanishi, K.1    Kamikubo, T.2    Matsuno, R.3
  • 210
    • 0000862208 scopus 로고
    • Peptide syntheses with proteinases. Fragment condensation of ZLeuGlnGlyOH or ZGlnGlyOH with HLeuValNH2 using metalloproteinases
    • 2 using metalloproteinases, Bull. Chem. Soc. Jpn., 51, 271, 1978.
    • (1978) Bull. Chem. Soc. Jpn. , vol.51 , pp. 271
    • Isowa, Y.1    Ichikawa, T.2    Ohmori, M.3
  • 211
  • 212
    • 0018635513 scopus 로고
    • Enzymatic synthesis of Leu- and Met-enkephalin
    • Kullniann, W., Enzymatic synthesis of Leu- and Met-enkephalin, Biochem. Biophys. Res. Commun., 91, 693, 1979.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 693
    • Kullniann, W.1
  • 213
    • 0019203667 scopus 로고
    • Proteases as catalysts of enzymic syntheses of opioid peptides
    • Kullmann, W., Proteases as catalysts of enzymic syntheses of opioid peptides, J. Biol. Chem., 255, 8234, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8234
    • Kullmann, W.1
  • 214
    • 0014397138 scopus 로고
    • Peptide synthesis via oxidation of A'-acyl-a-amino acid phenylhy-drazides. III. Dialanyl-insulin and diphenylalanyl-insulin
    • Milne, H. B. and Carpenter, F. H., Peptide synthesis via oxidation of A'-acyl-a-amino acid phenylhy-drazides. III. Dialanyl-insulin and diphenylalanyl-insulin, J. Org. Chem., 33, 4476, 1968.
    • (1968) J. Org. Chem. , vol.33 , pp. 4476
    • Milne, H.B.1    Carpenter, F.H.2
  • 215
    • 0010561365 scopus 로고
    • Peptide synthesis via oxidation of A'-acetyl-a-amino acid phenylhydrazides
    • Milne, H. B. and Kiidey, W., Peptide synthesis via oxidation of A'-acetyl-a-amino acid phenylhydrazides, J. Org. Chem., 30, 64, 1965.
    • (1965) J. Org. Chem. , vol.30 , pp. 64
    • Milne, H.B.1    Kiidey, W.2
  • 216
    • 77956993021 scopus 로고
    • N-bromosuccinimide cleavage of peptides
    • Ramachandran, L. K. and Witkop, B., N-bromosuccinimide cleavage of peptides, Methods Enzymol., 11, 283, 1967.
    • (1967) Methods Enzymol , vol.11 , pp. 283
    • Ramachandran, L.K.1    Witkop, B.2
  • 217
    • 33947472741 scopus 로고
    • The a-chymotrypsin-catalyzed hydrolysis of a-N and O-alkyl derivatives of ct-N-acetyl-L-tyrosine methyl ester
    • Peterson, R. L., Hubele, K. W., and Niemann, C., The a-chymotrypsin-catalyzed hydrolysis of a-N and O-alkyl derivatives of ct-N-acetyl-L-tyrosine methyl ester, Biochemistry,2, 942. 1963.
    • (1963) Biochemistry , vol.2 , pp. 942
    • Peterson, R.L.1    Hubele, K.W.2    Niemann, C.3
  • 218
    • 0022071866 scopus 로고
    • Synthesis of leucine- and methionine-enkephalin using papain (In Russian)
    • Zapevalova, N. P., Gorbunova, E. Y., and Mitin, Y. V., Synthesis of leucine- and methionine-enkephalin using papain (in Russian), Bioorg. Khim., 11, 733, 1985.
    • (1985) Bioorg. Khim. , vol.11 , pp. 733
    • Zapevalova, N.P.1    Gorbunova, E.Y.2    Mitin, Y.V.3
  • 220
    • 84914556676 scopus 로고
    • Carboxypeptidase Y as a catalyst for peptide synthesis in aqueous phase with minimal protection
    • Brunfeldt, K., Ed., Scriptor, Kopenhagen
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y as a catalyst for peptide synthesis in aqueous phase with minimal protection, in Peptides 1980, Proc. 16th Europ. Peptide Symp., Brunfeldt, K., Ed., Scriptor, Kopenhagen, 1981, 46.
    • (1981) Peptides 1980, Proc. 16Th Europ. Peptide Symp , pp. 46
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 221
    • 0000990957 scopus 로고
    • Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components, Carlsberg Res. Commun., 45, 453, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 453
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 222
    • 0011300588 scopus 로고
    • Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis
    • Breddam, K., Widmer, F., and Johansen, J. T., Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis, Carlsberg Res. Commun., 45, 237, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 237
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 223
    • 0021362657 scopus 로고
    • Design, synthesis, and binding properties of an opiate receptor mimetic peptide
    • Kulimann, W., Design, synthesis, and binding properties of an opiate receptor mimetic peptide, J. Med. Chem., 27, 106, 1984.
    • (1984) J. Med. Chem. , vol.27 , pp. 106
    • Kulimann, W.1
  • 224
    • 0019790314 scopus 로고
    • Biological inactivation of enkephalins and the role of enkephalin-dipeptidyl-carboxypeptidase (“Enkephalinase”) as neuropeptidase
    • Schwartz, J.-C., Malfroy, B., and De La Baume, S., Biological inactivation of enkephalins and the role of enkephalin-dipeptidyl-carboxypeptidase (“Enkephalinase”) as neuropeptidase, Life Sei., 29, 1715, 1981.
    • (1981) Life Sei. , vol.29 , pp. 1715
    • Schwartz, J.-C.1    Malfroy, B.2    De La Baume, S.3
  • 225
    • 0020446397 scopus 로고
    • Synthesis and pharmacological characterization in vitro of cyclic enkephalin analogues: Effect of conformational constraints on opiate receptor selectivity
    • Di Maio, J., Nguyen, T.M.-D., Lemieux, C., and Schiller, P. W., Synthesis and pharmacological characterization in vitro of cyclic enkephalin analogues: effect of conformational constraints on opiate receptor selectivity, J. Med. Chem., 25, 1432, 1982.
    • (1982) J. Med. Chem. , vol.25 , pp. 1432
    • Di Maio, J.1    Nguyen, T.M.2    Lemieux, C.3    Schiller, P.W.4
  • 226
    • 0038290652 scopus 로고
    • Opioid receptors
    • Gross, E., Meienhofer, J., and Hruby, V., Eds., Academic Press, New York
    • Paterson, S. J., Robson, L. E., and Kosterlitz, H. W., Opioid receptors, in The Peptides, Vol. 6, Gross, E., Meienhofer, J., and Hruby, V., Eds., Academic Press, New York, 1984, 147.
    • (1984) The Peptides , vol.6 , pp. 147
    • Paterson, S.J.1    Robson, L.E.2    Kosterlitz, H.W.3
  • 227
    • 0021953428 scopus 로고
    • Chemical-enzymatic incorporation of D-amino acids into peptides: Synthesis of diastereomeric (D-Ala2, D-Leu5) enkephalinamides
    • 5) enkephalinamides, FEBS Lett., 183, 103, 1985.
    • (1985) FEBS Lett. , vol.183 , pp. 103
    • Stoineva, E.B.1    Petkov, D.D.2
  • 228
    • 0000636758 scopus 로고
    • Enzyme peptide synthesis by an iterative procedure in a nucleophile pool
    • Petkov, D. D. and Stoineva, I. B., Enzyme peptide synthesis by an iterative procedure in a nucleophile pool, Tetrahedron Lett., 25, 3751, 1984.
    • (1984) Tetrahedron Lett. , vol.25 , pp. 3751
    • Petkov, D.D.1    Stoineva, I.B.2
  • 229
    • 0017379736 scopus 로고
    • A-Chymotrypsin as the catalyst for peptide synthesis
    • Morihara, K. and Oka, T., a-Chymotrypsin as the catalyst for peptide synthesis, Biochem. J., 163, 531, 1977.
    • (1977) Biochem. J. , vol.163 , pp. 531
    • Morihara, K.1    Oka, T.2
  • 230
    • 85054406937 scopus 로고    scopus 로고
    • unpublished results
    • Kullmann, W., unpublished results.
    • Kullmann, W.1
  • 231
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 232
    • 0020359083 scopus 로고
    • Enzymatic synthesis of dynorphin(L-8)
    • Kullmann, W., Enzymatic synthesis of dynorphin(l-8), J. Org. Chem., 47, 5300, 1982.
    • (1982) J. Org. Chem. , vol.47 , pp. 5300
    • Kullmann, W.1
  • 234
    • 0019805925 scopus 로고
    • Evidence for the occurrence of the opioid octapeptide dynorphin (1-8) in the neurointermediate pituitary of rats
    • Seizlnger, B. R., Höllt, V., and Hertz, A., Evidence for the occurrence of the opioid octapeptide dynorphin (1-8) in the neurointermediate pituitary of rats, Biochem. Biophys. Res. Commun., 102, 197, 1981.
    • (1981) Biochem. Biophys. Res. Commun. , vol.102 , pp. 197
    • Seizlnger, B.R.1    Höllt, V.2    Hertz, A.3
  • 236
    • 0020079125 scopus 로고
    • Isolation and structure of dynorphin, an opioid peptide from porcine duodenum
    • Tachibana, S., Araki, K., Ohya, S., and Yoshida, S., Isolation and structure of dynorphin, an opioid peptide from porcine duodenum, Nature (London),295, 339, 1982.
    • (1982) Nature (London) , vol.295 , pp. 339
    • Tachibana, S.1    Araki, K.2    Ohya, S.3    Yoshida, S.4
  • 237
    • 0345158331 scopus 로고
    • Specific receptor for the opioid peptide dynorphin: Structure-activity relationships
    • Chavkin, C. and Goldstein, A., Specific receptor for the opioid peptide dynorphin: structure-activity relationships, Proc. Natl. Acad. Sei. U.S.A., 78, 6543, 1981.
    • (1981) Proc. Natl. Acad. Sei. U.S.A. , vol.78 , pp. 6543
    • Chavkin, C.1    Goldstein, A.2
  • 239
    • 85004754595 scopus 로고
    • Side-reactions in peptide synthesis
    • Bodanszky, M. and Martinek, J., Side-reactions in peptide synthesis, Synthesis,333, 1981.
    • (1981) Synthesis , pp. 333
    • Bodanszky, M.1    Martinek, J.2
  • 240
    • 0010729788 scopus 로고
    • Amine protecting groups
    • Gross, E. and Meienhofer, J., Eds., Academic Press, New York
    • Geiger, R. and König, W., Amine protecting groups, in The Peptides, Vol. 3, Gross, E. and Meienhofer, J., Eds., Academic Press, New York, 1981, 1.
    • (1981) The Peptides , vol.3 , pp. 1
    • Geiger, R.1    König, W.2
  • 241
    • 0001926444 scopus 로고
    • Gross, E. and Meienhofer, J., Eds., Academic Press, New York
    • Barany, G. and Merrifield, R. B., Solid phase synthesis, in The Peptides, Vol. 2, Gross, E. and Meienhofer, J., Eds., Academic Press, New York, 1980, 1.
    • (1980) The Peptides , vol.2 , pp. 1
    • Barany, G.1    Merrifield, R.2
  • 243
    • 0014421640 scopus 로고
    • Structure of porcine cholecystokinin-pancreozymin
    • Mutt, V. and Jorpes, J. E., Structure of porcine cholecystokinin-pancreozymin, Eur. J. Biochem., 6, 156, 1968.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 156
    • Mutt, V.1    Jorpes, J.E.2
  • 244
    • 0012604455 scopus 로고
    • Protease-catalyzed peptide bond formation: Application to synthesis of the COOH-terminal octapeptide of cholecystokinin
    • Kullmann, W., Protease-catalyzed peptide bond formation: application to synthesis of the COOH-terminal octapeptide of cholecystokinin, Proc. Natl. Acad. Sei. U.S.A., 79, 2840, 1982.
    • (1982) Proc. Natl. Acad. Sei. U.S.A. , vol.79 , pp. 2840
    • Kullmann, W.1
  • 245
    • 0014206556 scopus 로고
    • Isolation and structure of caerulein, an active decapeptide from the skin of Hyla caerulea
    • Anastasi, A., Erspamer, V., and Endean, R., Isolation and structure of caerulein, an active decapeptide from the skin of Hyla caerulea, Experientia,23, 699, 1967.
    • (1967) Experientia , vol.23 , pp. 699
    • Anastasi, A.1    Erspamer, V.2    Endean, R.3
  • 248
    • 0016376184 scopus 로고
    • Comparative specificity of microbial proteinases
    • Morihara, K., Comparative specificity of microbial proteinases, Adv. Enzymol. Relat. Areas Mol. Biol., 41, 179, 1974.
    • (1974) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.41 , pp. 179
    • Morihara, K.1
  • 249
    • 0017063194 scopus 로고
    • Specificity of acid proteinase A from Aspergillus niger var. Macrosporus towards B-chain of performic acid oxidized insulin
    • Iio, I. and Yamasaki, M., Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized insulin, Biochim. Biophys. Acta,429, 912, 1976.
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 912
    • Iio, I.1    Yamasaki, M.2
  • 250
    • 0021019341 scopus 로고
    • Protease-catalyzed synthesis of melanocyte-stimulating hormone (MSH) fragments
    • Kullmann, W., Protease-catalyzed synthesis of melanocyte-stimulating hormone (MSH) fragments, J. Protein Chem., 2, 289, 1983.
    • (1983) J. Protein Chem. , vol.2 , pp. 289
    • Kullmann, W.1
  • 252
    • 85054409047 scopus 로고    scopus 로고
    • National Biomedical Research Foundation, Washington, D.C., 1972, D-194
    • Dayhoff, M. O., Atlas of Protein Sequence and Structure, Vol. 5, National Biomedical Research Foundation, Washington, D.C., 1972, D-194.
    • Atlas of Protein Sequence and Structure , vol.5
    • Dayhoff, M.O.1
  • 253
    • 84916704218 scopus 로고
    • Syntheses of peptides related to the N-terminal structure of corticotropin. III. The synthesis of L-histidyl-L-phenylalanyl-L-arginyl-L-tryptophan, the smallest peptide exhibiting the melanocyte-stimulating and the lipolytic activities
    • Otsuka, H. and Inouye, K., Syntheses of peptides related to the N-terminal structure of corticotropin. III. The synthesis of L-histidyl-L-phenylalanyl-L-arginyl-L-tryptophan, the smallest peptide exhibiting the melanocyte-stimulating and the lipolytic activities. Bull. Chem. Soc. Jpn., 37, 1465, 1964.
    • (1964) Bull. Chem. Soc. Jpn. , vol.37 , pp. 1465
    • Otsuka, H.1    Inouye, K.2
  • 254
    • 0006645810 scopus 로고
    • Studies on polypeptides. X. The synthesis of a pentapeptide corresponding to an amino acid sequence present in corticotropin and in the melanocyte stimulating hormones
    • Hofmann, K., Woolner, M. E., Spühler, G., and Schwartz, E. T., Studies on polypeptides. X. The synthesis of a pentapeptide corresponding to an amino acid sequence present in corticotropin and in the melanocyte stimulating hormones, J. Am. Chem. Soc., 80, 1486, 1958.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 1486
    • Hofmann, K.1    Woolner, M.E.2    Spühler, G.3    Schwartz, E.T.4
  • 255
    • 36949073223 scopus 로고
    • A new synthesis of the pentapeptide L-histidyl-L-phenylalanyl-L-arginyl-L-tryptophyl-glycine and its melanocyte-stimulating activity
    • Schwyzer, R. and Li, C. H., A new synthesis of the pentapeptide L-histidyl-L-phenylalanyl-L-arginyl-L-tryptophyl-glycine and its melanocyte-stimulating activity, Nature (London),182, 1669, 1958.
    • (1958) Nature (London) , vol.182 , pp. 1669
    • Schwyzer, R.1    Li, C.H.2
  • 256
    • 33947449457 scopus 로고
    • Phenylalanylphenylalanine ethyl ester synthesis
    • Tauber, H., Phenylalanylphenylalanine ethyl ester synthesis, J. Am. Chem. Soc., 74, 847, 1952.
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 847
    • Tauber, H.1
  • 257
    • 84985059113 scopus 로고
    • Papain-induced oligomerization of amino acid esters
    • Anderson, G. and Luisi, P. L., Papain-induced oligomerization of amino acid esters, Helv. Chim. Acta, 62, 488, 1979.
    • (1979) Helv. Chim. Acta , vol.62 , pp. 488
    • Anderson, G.1    Luisi, P.L.2
  • 258
    • 0000816516 scopus 로고
    • Syntheses of -V-acyl dipeptide derivatives by metalloproteinases
    • Isowa, Y. and Ichikawa, T., Syntheses of -V-acyl dipeptide derivatives by metalloproteinases, Bull. Chem. Soc. Jpn., 52, 796, 1979.
    • (1979) Bull. Chem. Soc. Jpn. , vol.52 , pp. 796
    • Isowa, Y.1    Ichikawa, T.2
  • 259
    • 0016186591 scopus 로고
    • Structural studies of a-melanocyte-stimulating hormone and a novel ß-melanocyte-stimulating hormone from the neurointermediate lobe of the pituitary of the dogfish squalus acanthias
    • Bennett, H. P. L., Lowry, P. J., McMartin, C., and Scott, A. P., Structural studies of a-melanocyte-stimulating hormone and a novel ß-melanocyte-stimulating hormone from the neurointermediate lobe of the pituitary of the dogfish squalus acanthias, Biochem. J., 141, 439, 1974.
    • (1974) Biochem. J. , vol.141 , pp. 439
    • Bennett, H.P.L.1    Lowry, P.J.2    McMartin, C.3    Scott, A.P.4
  • 260
    • 0343018214 scopus 로고
    • Synthese von N-geschiitztem Eledoisin(6-11)-Hexapeptid unter Verwendung von Proteasen als Biokatalysatoren
    • Kuhl, P., Döring, G., Neubert, K., and Jakubke, H.-D., Synthese von N-geschiitztem Eledoisin(6-11)-Hexapeptid unter Verwendung von Proteasen als Biokatalysatoren, Monatsh. Chem., 115, 423, 1984.
    • (1984) Monatsh. Chem. , vol.115 , pp. 423
    • Kuhl, P.1    Döring, G.2    Neubert, K.3    Jakubke, H.-D.4
  • 261
    • 0019879061 scopus 로고
    • Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift
    • Martinek, K., Semenov, A. N., and Berezin, I. V., Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift, Biochim. Biophys. Acta,658, 76, 1981.
    • (1981) Biochim. Biophys. Acta , vol.658 , pp. 76
    • Martinek, K.1    Semenov, A.N.2    Berezin, I.V.3
  • 262
    • 84913714366 scopus 로고
    • Untersuchungen zum Einfluss der Reaktionsbedingungen auf die a-chymotrypsinkatalysierte Peptidsynthese im wässrig-organischen Zweiphasensystem
    • Kuhl, P., Walpuski, J., and Jakubke, H.-D., Untersuchungen zum Einfluss der Reaktionsbedingungen auf die a-chymotrypsinkatalysierte Peptidsynthese im wässrig-organischen Zweiphasensystem, Pharmazie, 37, 766, 1982.
    • (1982) Pharmazie , vol.37 , pp. 766
    • Kuhl, P.1    Walpuski, J.2    Jakubke, H.-D.3
  • 263
  • 264
    • 0015502174 scopus 로고
    • The primary structure of epidermal growth factor
    • Savage, C. R., Jr., Inagami, T., and Cohen, S., The primary structure of epidermal growth factor, J. Biol. Chem., 247, 7612, 1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7612
    • Savage, C.R.1    Inagami, T.2    Cohen, S.3
  • 265
    • 0015758018 scopus 로고
    • Epidermic growth factor. Location of disulfide bonds
    • Savage, C. R., Jr., Hash, J. H., and Cohen, S., Epidermic growth factor. Location of disulfide bonds, J. Biol. Chem., 248, 7669, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7669
    • Savage, C.R.1    Hash, J.H.2    Cohen, S.3
  • 266
    • 0016719486 scopus 로고
    • Isolation and structure of urogastrone and its relationship to epidermal growth factor
    • Gregory, H., Isolation and structure of urogastrone and its relationship to epidermal growth factor, Nature (London),257, 325, 1975.
    • (1975) Nature (London) , vol.257 , pp. 325
    • Gregory, H.1
  • 267
    • 0021364168 scopus 로고
    • Biologically active synthetic fragments of epidermal growth factor: Localization of a major receptor binding region
    • Komoriya, A., Mortsch, M., Meyers, C., Smith, M., Kanety, H., and Sclesinger, J., Biologically active synthetic fragments of epidermal growth factor: localization of a major receptor binding region, Proc. Natl. Acad. Sei. U.S.A., 81, 1351, 1984.
    • (1984) Proc. Natl. Acad. Sei. U.S.A. , vol.81 , pp. 1351
    • Komoriya, A.1    Mortsch, M.2    Meyers, C.3    Smith, M.4    Kanety, H.5    Sclesinger, J.6
  • 269
    • 85023505997 scopus 로고
    • Reversible zymo-hydrolysis
    • Elsevier, Amsterdam
    • Florkin, M. and Stotz, E. H., Reversible zymo-hydrolysis, in Comprehensive Biochemistry, Vol. 32, Elsevier, Amsterdam, 1977, 307.
    • (1977) Comprehensive Biochemistry , vol.32 , pp. 307
    • Florkin, M.1    Stotz, E.H.2
  • 270
    • 0039663046 scopus 로고
    • Über die enzymatische Polypeptidsynthese
    • Virtanen, A. I., Über die enzymatische Polypeptidsynthese, Makromol. Chem., 6, 94, 1951.
    • (1951) Makromol. Chem. , vol.6 , pp. 94
    • Virtanen, A.I.1
  • 271
    • 84982059488 scopus 로고
    • Isolierung einheitlicher Plastein-Bausteine
    • Wieland, T., Determann, H., and Albrecht, E., Untersuchungen über die Plastein-Reaktion. Isolierung einheitlicher Plastein-Bausteine, Justus Liebigs Ann. Chem.633, 185, 1960.
    • (1960) Justus Liebigs Ann. Chem. , vol.633 , pp. 185
    • Wieland, T.1    Determann, H.2    Albrecht, E.3
  • 272
    • 85054410787 scopus 로고
    • Ein synthetisches Pentapeptid als Plastein-Monomeres. Untersuchungen über die Plastein-Reaktion. II
    • Determann, H. and Wieland, T., Ein synthetisches Pentapeptid als Plastein-Monomeres. Untersuchungen über die Plastein-Reaktion. II, Makromol. Chem., 44-46, 312, 1961.
    • (1961) Makromol. Chem. , vol.312 , pp. 44-46
    • Determann, H.1    Wieland, T.2
  • 273
    • 84957220745 scopus 로고
    • Untersuchungen über die Plastein-Reaktion. VI. Einfluss der Kettenlänge und der Endgruppen des Monomeren auf die Kondensierbarkeit
    • Determann, H., Bonhard, K., Köhler, R., and Wieland, T., Untersuchungen über die Plastein-Reaktion. VI. Einfluss der Kettenlänge und der Endgruppen des Monomeren auf die Kondensierbarkeit, Helv. Chim. Acta,46, 2498, 1963.
    • (1963) Helv. Chim. Acta , vol.46 , pp. 2498
    • Determann, H.1    Bonhard, K.2    Köhler, R.3    Wieland, T.4
  • 274
    • 0013829309 scopus 로고
    • Spezifität des Pepsins bei der Kondensationsreaktion
    • Determann, H., Heuer, J., and Jaworek, D., Untersuchungen über die Plastein-Reaktion. VIII. Spezifität des Pepsins bei der Kondensationsreaktion, Justus Liebigs Ann. Chem., 690, 189, 1965.
    • (1965) Justus Liebigs Ann. Chem. , vol.690 , pp. 189
    • Determann, H.1    Heuer, J.2    Jaworek, D.3
  • 275
    • 0013839472 scopus 로고
    • Untersuchungen über die Plastein-Reaktion. VII. Molekulargewichtsverteilung des enzymatischen Kondensationsprodukts
    • Determann, H., Eggenschwiller, S., and Michel, W., Untersuchungen über die Plastein-Reaktion. VII. Molekulargewichtsverteilung des enzymatischen Kondensationsprodukts, Justus Liebigs Ann. Chem., 690, 182, 1965.
    • (1965) Justus Liebigs Ann. Chem. , vol.690 , pp. 182
    • Determann, H.1    Eggenschwiller, S.2    Michel, W.3
  • 276
    • 0002080621 scopus 로고
    • Enzymatic protein degradation and resynthesis for protein improvement
    • Fujimaki, M., Arai, S., and Yamashita, M., Enzymatic protein degradation and resynthesis for protein improvement, Adv. Chem. Series,160, 156, 1977.
    • (1977) Adv. Chem. Series , vol.160 , pp. 156
    • Fujimaki, M.1    Arai, S.2    Yamashita, M.3
  • 277
    • 33750082259 scopus 로고
    • Transamidation reactions catalyzed by cathepsin C
    • Jones, M. E., Hearn, W. R., Fried, M., and Fruton, J. S., Transamidation reactions catalyzed by cathepsin C, J. Biol. Chem., 195, 645, 1952.
    • (1952) J. Biol. Chem. , vol.195 , pp. 645
    • Jones, M.E.1    Hearn, W.R.2    Fried, M.3    Fruton, J.S.4
  • 278
    • 0009703932 scopus 로고
    • Synthesis of polymeric peptides in proteinase-catalyzed transamidation reactions
    • Fruton, J. S., Hearn, W. R., Ingram, V. M., Wiggans, D. S., and Winitz, M., Synthesis of polymeric peptides in proteinase-catalyzed transamidation reactions, J. Biol. Chem., 204, 891, 1953.
    • (1953) J. Biol. Chem. , vol.204 , pp. 891
    • Fruton, J.S.1    Hearn, W.R.2    Ingram, V.M.3    Wiggans, D.S.4    Winitz, M.5
  • 279
    • 0002999545 scopus 로고
    • Specificity of cathepsin C
    • Izymiya, N., and Fruton, J. S., Specificity of cathepsin C, J. Biol. Chem., 218, 59, 1956.
    • (1956) J. Biol. Chem. , vol.218 , pp. 59
    • Izymiya, N.1    Fruton, J.S.2
  • 280
    • 33750044261 scopus 로고
    • Polymerization of dipeptide amides by cathepsin C
    • Würz, H., Tanaka, A., and Fruton, J. S., Polymerization of dipeptide amides by cathepsin C, Biochemistry,1, 19, 1962.
    • (1962) Biochemistry , vol.1 , pp. 19
    • Würz, H.1    Tanaka, A.2    Fruton, J.S.3
  • 281
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 285
    • 84981840591 scopus 로고
    • Enzymatische Peptidsynthese. Isolierung von enzymatisch gebildetem L-Methionyl-L-methionin und L-Methionyl-L-methionyl-L-methionin; Vergleich mit synthetischen Produkten
    • Brenner, M. and Pfister, R. W., Enzymatische Peptidsynthese. Isolierung von enzymatisch gebildetem L-Methionyl-L-methionin und L-Methionyl-L-methionyl-L-methionin; Vergleich mit synthetischen Produkten, Helv. Chim. Acta,34, 2085, 1951.
    • (1951) Helv. Chim. Acta , vol.34 , pp. 2085
    • Brenner, M.1    Pfister, R.W.2
  • 286
    • 84981834827 scopus 로고
    • Enzymatische Peptidsynthese. Peptidbildung aus DL-Threonin-isopropylester
    • Brenner, M., Sailer, E., and Rüfenacht, K., Enzymatische Peptidsynthese. Peptidbildung aus DL-Threonin-isopropylester, Helv. Chim. Acta,34, 2096, 1951.
    • (1951) Helv. Chim. Acta , vol.34 , pp. 2096
    • Brenner, M.1    Sailer, E.2    Rüfenacht, K.3
  • 287
    • 84985059113 scopus 로고
    • Papain-induced oligomerization of a-amino acid esters
    • Anderson, G. and Luisi, P. L., Papain-induced oligomerization of a-amino acid esters, Helv. Chim. Acta, 62, 488, 1979.
    • (1979) Helv. Chim. Acta , vol.62 , pp. 488
    • Anderson, G.1    Luisi, P.L.2
  • 288
    • 84985108854 scopus 로고
    • Papain-catalyzed oligomerization of a-amino acids. Synthesis and characterization of water-insoluble oligomers of L-methionine
    • Jost, R., Brambilla, E., Monti, J. C., and Luisi, P. L., Papain-catalyzed oligomerization of a-amino acids. Synthesis and characterization of water-insoluble oligomers of L-methionine, Helv. Chim. Acta, 63, 375, 1980.
    • (1980) Helv. Chim. Acta , vol.63 , pp. 375
    • Jost, R.1    Brambilla, E.2    Monti, J.3    Luisi, C.P.L.4
  • 289
    • 0000990957 scopus 로고
    • Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components, Carlsberg Res. Commun., 45, 453, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 453
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 290
    • 84914556676 scopus 로고
    • Carboxypeptidase Y as catalyst for peptide synthesis in aqueous phase with minimal protection
    • Brunfeldt, K., Ed., Scriptor, Kopenhagen
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y as catalyst for peptide synthesis in aqueous phase with minimal protection, in Peptides 1980, Proc. 16th Eur. Peptide Symp., Brunfeldt, K., Ed., Scriptor, Kopenhagen, 1981, 46.
    • (1981) Peptides 1980, Proc. 16Th Eur. Peptide Symp , pp. 46
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 291
    • 0012606494 scopus 로고
    • Amino acid methyl esters as amine components in CPD-Y catalyzed peptide synthesis: Control of side-reactions
    • Breddam, K., Widmer, F., and Johansen, J. T., Amino acid methyl esters as amine components in CPD-Y catalyzed peptide synthesis: control of side-reactions, Carlsberg Res. Commun., 48, 231, 1983.
    • (1983) Carlsberg Res. Commun. , vol.48 , pp. 231
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 292
    • 0003511271 scopus 로고
    • The peptide bond
    • Gross, E. and Meienhofer, J., Eds., Academic Press, New York
    • Gross, E., and Meienhofer, J., The peptide bond, in The Peptides: Analysis, Synthesis, Biology, Vol.1, Gross, E. and Meienhofer, J., Eds., Academic Press, New York, 1979, 1.
    • (1979) The Peptides: Analysis, Synthesis, Biology , vol.1 , pp. 1
    • Gross, E.1    Meienhofer, J.2
  • 293
    • 0004726179 scopus 로고
    • Amino-acid sequence of human insulin
    • Nicol, D. S. H. W. and Smith, L. F., Amino-acid sequence of human insulin, Nature (London),187, 483, 1960.
    • (1960) Nature (London) , vol.187 , pp. 483
    • Nicol, D.S.H.W.1    Smith, L.F.2
  • 295
    • 0015514959 scopus 로고
    • Human insulin: Facile synthesis by modification of porcine insulin
    • Ruttenberg, M. A., Human insulin: facile synthesis by modification of porcine insulin. Science,177, 623, 1972.
    • (1972) Science , vol.177 , pp. 623
    • Ruttenberg, M.A.1
  • 296
    • 0017140646 scopus 로고
    • A new semisynthesis of human insulin, Hoppe Sexier's Z
    • Obermeier, R. and Geiger, R., A new semisynthesis of human insulin, Hoppe Sexier's Z. Physiol. Chem., 357, 759, 1976.
    • (1976) Physiol. Chem. , vol.357 , pp. 759
    • Obermeier, R.1    Geiger, R.2
  • 297
    • 84958255174 scopus 로고
    • The amino-acid sequence in the phenylalanyl chain of insulin
    • Sanger, F. and Tuppy, H., The amino-acid sequence in the phenylalanyl chain of insulin, Biochem. J., 49, 481, 1951.
    • (1951) Biochem. J. , vol.49 , pp. 481
    • Sanger, F.1    Tuppy, H.2
  • 298
    • 0001035679 scopus 로고
    • Isolation and characterization of products formed by the action of trypsin on insulin
    • Young, J. D. and Carpenter, F. H., Isolation and characterization of products formed by the action of trypsin on insulin, J. Biol. Chem., 236, 743, 1961.
    • (1961) J. Biol. Chem. , vol.236 , pp. 743
    • Young, J.D.1    Carpenter, F.H.2
  • 299
    • 33947462863 scopus 로고
    • The use of carboxypeptidase for the identification of terminal carboxyl groups in polypeptides and proteins. Asparagine as a C-terminal residue in insulin
    • Harris, J. J., The use of carboxypeptidase for the identification of terminal carboxyl groups in polypeptides and proteins. Asparagine as a C-terminal residue in insulin, J. Am. Chem. Soc., 74, 2944, 1952.
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 2944
    • Harris, J.J.1
  • 301
    • 0018421382 scopus 로고
    • Semisynthesis of human insulin by trypsin-catalyzed replacement of Ala-B 30 by Thr in porcine insulin
    • Morihara, K., Oka, T., and Tsuzuki, H., Semisynthesis of human insulin by trypsin-catalyzed replacement of Ala-B 30 by Thr in porcine insulin, Nature (London),280, 412, 1979.
    • (1979) Nature (London) , vol.280 , pp. 412
    • Morihara, K.1    Oka, T.2    Tsuzuki, H.3
  • 302
    • 84910434272 scopus 로고
    • Enzyme catalyzed semisynthesis with insulin derivatives
    • Aachen, W. Germany, 1979, Brandenburg, D. and Wollmer, A., Eds., Walter de Gruyter, Berlin
    • Gattner, H.-G., Danho, W., and Naithani, V. K., Enzyme catalyzed semisynthesis with insulin derivatives, in Proc. 2nd Int. Insulin Symp., Aachen, W. Germany, 1979, Brandenburg, D. and Wollmer, A., Eds., Walter de Gruyter, Berlin, 1980, 117.
    • (1980) Proc. 2Nd Int. Insulin Symp , pp. 117
    • Gattner, H.-G.1    Danho, W.2    Naithani, V.K.3
  • 304
    • 0019809497 scopus 로고
    • Eine neue Semisynthese des Humaninsulins. Tryptisch-katalysierte Transpeptidierung von Schweineinsulin mit L-Threonin-feri-butyl-ester
    • Jonczyk, K. A. and Gattner, H.-G., Eine neue Semisynthese des Humaninsulins. Tryptisch-katalysierte Transpeptidierung von Schweineinsulin mit L-Threonin-feri-butyl-ester, Hoppe Seyler’s Z. Phxsiol. Chem., 362, 1591, 1981.
    • (1981) Hoppe Seyler’s Z. Phxsiol. Chem. , vol.362 , pp. 1591
    • Jonczyk, K.A.1    Gattner, H.-G.2
  • 305
    • 3142553522 scopus 로고
    • Reaction mechanism in trypsin catalyzed synthesis of human insulin studied by 170-NMR spectroscopy
    • Blaha, K. and Malon, P., Eds., Walter de Gruyter, Berlin
    • 170-NMR spectroscopy, in Peptides 1982, 17th Eur. Peptide Symp., Blaha, K. and Malon, P., Eds., Walter de Gruyter, Berlin, 1983, 387.
    • (1983) Peptides 1982, 17Th Eur. Peptide Symp , pp. 387
    • Markussen, J.1    Schaumburg, K.2
  • 306
    • 0021236567 scopus 로고
    • A mass-spectrometric investigation of the mechanism of the semisynthetic transformation of pig insulin into an ester of insulin of human sequence
    • Rose, K., Gladstone, J., and Offord, R. E., A mass-spectrometric investigation of the mechanism of the semisynthetic transformation of pig insulin into an ester of insulin of human sequence. Biochem. J. 220, 189, 1984.
    • (1984) Biochem. J. , vol.220 , pp. 189
    • Rose, K.1    Gladstone, J.2    Offord, R.E.3
  • 307
    • 0020536517 scopus 로고
    • Rapid preparation of human insulin and insulin analogues in high yield by enzyme-assisted semi-synthesis
    • Rose, K., de Pury, H., and Offord, R. E., Rapid preparation of human insulin and insulin analogues in high yield by enzyme-assisted semi-synthesis, Biochem. J., 211, 671. 1983.
    • (1983) Biochem. J. , vol.211 , pp. 671
    • Rose, K.1    De Pury, H.2    Offord, R.E.3
  • 308
    • 0018077688 scopus 로고
    • A new proteolytic enzyme from Achromohacter lyticus M 497-1
    • Masaki, T., Nakamura, K., Isono, M., and Soejima, M., A new proteolytic enzyme from Achromohacter lyticus M 497-1, Agric. Biol. Chem., 42, 1443, 1978.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 1443
    • Masaki, T.1    Nakamura, K.2    Isono, M.3    Soejima, M.4
  • 309
  • 310
    • 26844564032 scopus 로고
    • Enzymatic semisynthesis of human insulin by transpeptidation method with Achromohacter protease: Comparison with the coupling method
    • Sakakibara, S., Ed., Protein Research Foundation, Osaka. Japan
    • Morihara, K. and Oka, T., Enzymatic semisynthesis of human insulin by transpeptidation method with Achromohacter protease: comparison with the coupling method, in Peptide Chemistry 1982, Sakakibara, S., Ed., Protein Research Foundation, Osaka. Japan, 1983, 231.
    • (1983) Peptide Chemistry 1982 , pp. 231
    • Morihara, K.1    Oka, T.2
  • 311
    • 85010123970 scopus 로고
    • Peptide synthesis using enzyme as synthetic catalyst — synthesis of new water-soluble ester substrates and enzyme immobilization-
    • Muneyuki, R., Oka, T., and Morihara, K., Peptide synthesis using enzyme as synthetic catalyst — synthesis of new water-soluble ester substrates and enzyme immobilization-, Nippon Kagukti Kuishi,1336, 1983.
    • (1983) Nippon Kagukti Kuishi , pp. 1336
    • Muneyuki, R.1    Oka, T.2    Morihara, K.3
  • 312
    • 84887070707 scopus 로고
    • Enzymatic semisynthesis of human insulin: A proposed procedure using immobilized enzyme
    • Hruby, V. J. and Rich, D. H., Eds., Pierce Chem., Rockfort
    • Oka, T., Muneyuki, R., and Morihara, K., Enzymatic semisynthesis of human insulin: a proposed procedure using immobilized enzyme, in Peptides, Structure and Function, Proc. 8th Am. Peptide Symp. Hruby, V. J. and Rich, D. H., Eds., Pierce Chem., Rockfort. 3., 1983, 199.
    • (1983) Peptides, Structure and Function, Proc. 8Th Am. Peptide Symp , vol.3 , pp. 199
    • Oka, T.1    Muneyuki, R.2    Morihara, K.3
  • 313
    • 3142578831 scopus 로고
    • Carboxypeptidase Y catalyzed C-terminal modification in the B-chain of porcine insulin
    • Breddam, K., Widmer, F., and Johansen, J. T., Carboxypeptidase Y catalyzed C-terminal modification in the B-chain of porcine insulin, Carlsberg Res. Commun., 46, 361, 1981.
    • (1981) Carlsberg Res. Commun. , vol.46 , pp. 361
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 314
    • 0011300588 scopus 로고
    • Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis
    • Breddam, K., Widmer, F., and Johansen, J. T., Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis, Carlsberg Res. Commun., 45, 237, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 237
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 315
    • 52449144823 scopus 로고
    • Semisynthesis of human insulin utilizing chemically modified carboxypeptidase Y
    • Breddam, K., and Johansen, J. T., Semisynthesis of human insulin utilizing chemically modified carboxypeptidase Y, Carlsberg Res. Commun., 49, 463, 1984.
    • (1984) Carlsberg Res. Commun. , vol.49 , pp. 463
    • Breddam, K.1    Johansen, J.T.2
  • 316
    • 0016920172 scopus 로고
    • Structure and activity of insulin. XIV. Further studies on the three-step-increase in activity due to the aromatic amino acids B24-26 (-Phe-Phe-Tyr-), Hoppe Sexier’s Z
    • Weitzel, G., Bauer, F., and Eisele, K., Structure and activity of insulin. XIV. Further studies on the three-step-increase in activity due to the aromatic amino acids B24-26 (-Phe-Phe-Tyr-), Hoppe Sexier’s Z. Physiol. Chem., 357, 187, 1976.
    • (1976) Physiol. Chem. , vol.357 , pp. 187
    • Weitzel, G.1    Bauer, F.2    Eisele, K.3
  • 317
    • 77956751025 scopus 로고
    • Insulin: The structure in the crystal and its reflection in chemistry and biology
    • Blundell, T. L., Dodson, G. G., Hodgkin, D. C., and Mercola, D. A., Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv. Prot. Chem., 26, 279, 1972.
    • (1972) Adv. Prot. Chem. , vol.26 , pp. 279
    • Blundell, T.L.1    Dodson, G.G.2    Hodgkin, D.C.3    Mercola, D.A.4
  • 319
    • 0019311259 scopus 로고
    • The preparation of two mutant forms of human insulin, containing leucine in position B 24 or B 25, by enzyme-assisted synthesis
    • Gattner, H.-G., Danho, W., Behn, C., and Zahn, H., The preparation of two mutant forms of human insulin, containing leucine in position B 24 or B 25, by enzyme-assisted synthesis. Hoppe Sexier’s Z. Physiol. Chem., 361, 1135, 1980.
    • (1980) Hoppe Sexier’s Z. Physiol. Chem. , vol.361 , pp. 1135
    • Gattner, H.-G.1    Danho, W.2    Behn, C.3    Zahn, H.4
  • 321
    • 84933790739 scopus 로고
    • Trypsin catalyzed peptide synthesis: Modification of the B-chain C-terminal region of insulin
    • Brunfeldt, K., Ed., ScriptorCopenhagen
    • Gattner, H.-D., Danho, W., Knorr, R., Naithani, V. K., and Zahn, H., Trypsin catalyzed peptide synthesis: modification of the B-chain C-terminal region of insulin, in Peptides 1980, Proc. 16th Eur. Peptide Symp. Brunfeldt, K., Ed., Scriptor, Copenhagen, 1981, 372.
    • (1981) Peptides 1980, Proc. 16Th Eur. Peptide Symp , pp. 372
    • Gattner, H.-D.1    Danho, W.2    Knorr, R.3    Naithani, V.K.4    Zahn, H.5
  • 324
    • 85021607793 scopus 로고
    • Semisynthesis of human insulin analogues containing a D-amino acid residue in position B 24, B 25, or B 26
    • Sakakibara, S., Ed., Protein Research Foundation, Osaka, Japan
    • Inouye, K., Watanabe, K., Tochino, Y., Kobayashi, M., Shigeta, Y., Semisynthesis of human insulin analogues containing a D-amino acid residue in position B 24, B 25, or B 26, in Peptide Chemistry 1982, Sakakibara, S., Ed., Protein Research Foundation, Osaka, Japan, 1983, 277.
    • (1983) Peptide Chemistry 1982 , pp. 277
    • Inouye, K.1    Watanabe, K.2    Tochino, Y.3    Kobayashi, Y.4    Shigeta, Y.5
  • 326
    • 0019797263 scopus 로고
    • Enzymatic synthesis of deshexapeptide insulin
    • Cao, Q. P., Cui, D. F., and Zhang, Y. S., Enzymatic synthesis of deshexapeptide insulin, Nature (London), 292, 774, 1981.
    • (1981) Nature (London) , vol.292 , pp. 774
    • Cao, Q.P.1    Cui, D.2    Zhang, F.Y.S.3
  • 327
    • 0019411277 scopus 로고
    • Intramolecular enzymatic peptide synthesis: Trypsinmediated coupling of the peptide bond between B22-arginine and B23-glycine in a split crosslinked insulin
    • Chu, S.-C., Wang, C.-C., and Brandenburg, D., Intramolecular enzymatic peptide synthesis: trypsinmediated coupling of the peptide bond between B22-arginine and B23-glycine in a split crosslinked insulin. Hoppe Sexier's Z. Physiol. Chem., 362, 647, 1981.
    • (1981) Hoppe Sexier's Z. Physiol. Chem. , vol.362 , pp. 647
    • Chu, S.-C.1    Wang, C.-C.2    Brandenburg, D.3
  • 329
    • 0015576315 scopus 로고
    • Studies on soybean trypsin inhibitors. III. Amino-acid sequence of the carboxyl-terminal region and the complete amino-acid sequence of soybean trypsin inhibitor (Kunitz)
    • Koide, T., and Ikenaka, T., Studies on soybean trypsin inhibitors. III. Amino-acid sequence of the carboxyl-terminal region and the complete amino-acid sequence of soybean trypsin inhibitor (Kunitz). Eur.J. Biochem.32, 417. 1973.
    • (1973) Eur.J. Biochem. , vol.32 , pp. 417
    • Koide, T.1    Ikenaka, T.2
  • 330
    • 0014011074 scopus 로고
    • The reactive site of trypsin inhibitor
    • Ozawa, K. and Laskowski, M., Jr., The reactive site of trypsin inhibitor. J. Biol. Chem.241, 3955, 1966.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3955
    • Ozawa, K.1    Laskowski, M.2
  • 331
    • 0016174105 scopus 로고
    • Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution
    • Sweet, R. M., Wright, H. T., Janin, J., Clothia, C. H., and Blow, D. M., Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution. Biochemistry,13. 4212, 1974.
    • (1974) Biochemistry , vol.13 , pp. 4212
    • Sweet, R.M.1    Wright, H.T.2    Janin, J.3    Clothia, C.H.4    Blow, D.M.5
  • 332
    • 0014578201 scopus 로고
    • Enzymatic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitor
    • Sealock, R. W. and Laskowski, M., Jr., Enzymatic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitor. Biochemistry.8. 3703. 1969.
    • (1969) Biochemistry. , vol.8 , pp. 3703
    • Sealock, R.W.1    Laskowski, M.2
  • 334
    • 0014216269 scopus 로고
    • Resynthesis by trypsin of the cleaved peptide bond in modified soybean trypsin inhibitor
    • Finkenstadt, R. and Laskowski, M., Jr., Resynthesis by trypsin of the cleaved peptide bond in modified soybean trypsin inhibitor, J. Biol. Chem., 242, 771, 1967.
    • (1967) J. Biol. Chem. , vol.242 , pp. 771
    • Finkenstadt, R.1    Laskowski, M.2
  • 335
    • 0015863122 scopus 로고
    • Enzymatic replacement of Arg„, by Trp„, in the reactive site of soybean trypsin inhibitor (Kunitz) — an intentional change from tryptic to chymotryptic specificity
    • Leary, T. R. and Laskowski, M., Jr., Enzymatic replacement of Arg„, by Trp„, in the reactive site of soybean trypsin inhibitor (Kunitz) — an intentional change from tryptic to chymotryptic specificity. Fed. Proc. Fed. Am. Soc. Exp. Biol., 32. 465, 1973.
    • (1973) Fed. Proc. Fed. Am. Soc. Exp. Biol. , vol.32 , pp. 465
    • Leary, T.R.1    Laskowski, M.2
  • 336
    • 0016176478 scopus 로고
    • Austausch von Lysin gegen Arginin. Phenylalanin und Tryptophan imreaktiven Zentrum des Trypsin-Kallikrein-lnhibitors (Kunitz)
    • Jering, H. and Tschesche, H., Austausch von Lysin gegen Arginin. Phenylalanin und Tryptophan imreaktiven Zentrum des Trypsin-Kallikrein-lnhibitors (Kunitz), Angew. Chem., 86. 704. 1974.
    • (1974) Angew. Chem. , vol.86 , pp. 704
    • Jering, H.1    Tschesche, H.2
  • 337
    • 0017295353 scopus 로고
    • Replacement of lysine by arginine, phenylalanine, and tryptophan in the reactive site of the bovine trypsin-kallikrein inhibitor (Kunitz) and change of the inhibitory properties
    • Jering, H. and Tschesche, H., Replacement of lysine by arginine, phenylalanine, and tryptophan in the reactive site of the bovine trypsin-kallikrein inhibitor (Kunitz) and change of the inhibitory properties, Eur. J. Biochem., 61, 453, 1976.
    • (1976) Eur. J. Biochem. , vol.61 , pp. 453
    • Jering, H.1    Tschesche, H.2
  • 338
    • 0001449760 scopus 로고
    • The basic trypsin inhibitor of bovine pancreas. IV. The linear sequence of the 58 amino acids
    • Kassell, B., Radicevic, M., Ansfield, M. J., and Laskowski, M., Sr., The basic trypsin inhibitor of bovine pancreas. IV. The linear sequence of the 58 amino acids. Biochem. Biophys. Res. Commun., 18, 255, 1965.
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 255
    • Kassell, B.1    Radicevic, M.2    Ansfield, M.J.3    Laskowski, M.4
  • 339
    • 0013849904 scopus 로고
    • The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages
    • Kassell, B. and Laskowski, M., Sr., The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages, Biochem. Biophys. Res. Commun., 20, 463, 1965.
    • (1965) Biochem. Biophys. Res. Commun. , vol.20 , pp. 463
    • Kassell, B.1    Laskowski, M.2
  • 340
    • 0016224696 scopus 로고
    • Darstellung des aktiven Derivates von Rinder-Trypsin-Kallikrein-Inhibitor (Kunitz) mit im aktiven Zentrum geöffneter Peptidbindung
    • Jering, H. and Tschesche, H., Darstellung des aktiven Derivates von Rinder-Trypsin-Kallikrein-Inhibitor (Kunitz) mit im aktiven Zentrum geöffneter Peptidbindung, Angew. Chem.86. 702. 1974.
    • (1974) Angew. Chem. , vol.86 , pp. 702
    • Jering, H.1    Tschesche, H.2
  • 341
    • 0017282087 scopus 로고
    • Preparation and characterization of the active derivative of bovine trypsinkallikrein inhibitor (Kunitz) with the reactive site lysine-15—alanine-16 hydrolyzed
    • Jering, H. and Tschesche, H., Preparation and characterization of the active derivative of bovine trypsinkallikrein inhibitor (Kunitz) with the reactive site lysine-15—alanine-16 hydrolyzed, Eur. J. Biochem., 61, 443, 1976.
    • (1976) Eur. J. Biochem. , vol.61 , pp. 443
    • Jering, H.1    Tschesche, H.2
  • 342
    • 0020651938 scopus 로고
    • Thermodynamics and kinetics of the hydrolysis and resynthesis of the reactive site peptide bond in turkey ovomucoid third domain by aspergillopeptidase B
    • Ardelt, W. and Laskowski, M., Jr., Thermodynamics and kinetics of the hydrolysis and resynthesis of the reactive site peptide bond in turkey ovomucoid third domain by aspergillopeptidase B, Acta Biochim. Polonica,30, 115, 1983.
    • (1983) Acta Biochim. Polonica , vol.30 , pp. 115
    • Ardelt, W.1    Laskowski, M.2
  • 343
    • 85023409682 scopus 로고
    • Limited proteolysis of ovomucoids caused by staphylococcal proteinase
    • Kato, J., Kohr, W. J., and Laskowski, M., Jr., Limited proteolysis of ovomucoids caused by staphylococcal proteinase. Fed. Proc. Fed. Am. Soc. Exp. Biol., 36, 764, 1977.
    • (1977) Fed. Proc. Fed. Am. Soc. Exp. Biol. , vol.36 , pp. 764
    • Kato, J.1    Kohr, W.J.2    Laskowski, M.3
  • 344
    • 0021111041 scopus 로고
    • Formation of covalent hybrids from amino-terminal and carboxy-terminal fragments of two ovomucoid third domains
    • Wieczorek, M. and Laskowski, M., Jr., Formation of covalent hybrids from amino-terminal and carboxy-terminal fragments of two ovomucoid third domains. Biochemistry.22, 2630, 1983.
    • (1983) Biochemistry , vol.22 , pp. 2630
    • Wieczorek, M.1    Laskowski, M.2
  • 345
    • 84965093921 scopus 로고
    • The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components
    • Richards, R. M. and Vithayathil, P. J., The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components, J. Biol. Chem., 234, 1459, 1959.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1459
    • Richards, R.M.1    Vithayathil, P.J.2
  • 346
    • 0018796243 scopus 로고
    • Enzymatic resynthesis of the hydrolyzed peptide bond(S) in ribonuclease S
    • Homandberg, G. A. and Laskowski, M. Jr., Enzymatic resynthesis of the hydrolyzed peptide bond(s) in ribonuclease S, Biochemistry.18, 586, 1979.
    • (1979) Biochemistry , vol.18 , pp. 586
    • Homandberg, G.A.1    Laskowski, M.2
  • 347
    • 84966403460 scopus 로고
    • Enzymatic conversion of selected noncovalent complexes of native or synthetic fragments to covalent forms
    • Gross. E. and Meienhofer, J., Eds. Pierce Chem., Rockford
    • Homandberg, G. A., Komoriya, A., Juillerat, M., and Chaiken, I. M., Enzymatic conversion of selected noncovalent complexes of native or synthetic fragments to covalent forms, in Peptides, Structure, and Biological Function, Gross. E. and Meienhofer, J., Eds. Pierce Chem., Rockford, 3., 1980. 597.
    • (1980) Peptides, Structure, and Biological Function , vol.3 , pp. 597
    • Homandberg, G.A.1    Komoriya, A.2    Juillerat, M.3    Chaiken, I.M.4
  • 349
    • 0020476104 scopus 로고
    • Enzymatic condensation of nonassociated peptide fragments using a molecular trap
    • Homandberg, G. A., Komoriya, A., and Chaiken, I. M., Enzymatic condensation of nonassociated peptide fragments using a molecular trap, Biochemistry,21, 3385, 1982.
    • (1982) Biochemistry , vol.21 , pp. 3385
    • Homandberg, G.A.1    Komoriya, A.2    Chaiken, I.M.3
  • 350
    • 0014430032 scopus 로고
    • Purification and properties of a clostridiopeptidase B (Clostripain)
    • Mitchel, W. M. and Harrington, W. F., Purification and properties of a clostridiopeptidase B (clostripain)J. Biol. Chem., 243, 4683, 1968.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4683
    • Mitchel, W.M.1    Harrington, W.F.2
  • 351
    • 0018883726 scopus 로고
    • Trypsin-catalyzed conversion of staphylococcal nuclease-T fragment complexes to covalent forms
    • Homandberg, G. A. and Chaiken, I. M., Trypsin-catalyzed conversion of staphylococcal nuclease-T fragment complexes to covalent forms. J. Biol. Chem., 255, 4903, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4903
    • Homandberg, G.A.1    Chaiken, I.M.2
  • 352
    • 0014126182 scopus 로고
    • Nuclease-T: An active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments
    • Taniuchi, H., Anfinsen, C. B., and Sodja, A., Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments, Proc. Natl. Acad. Sei. U.S.A., 58, 1235, 1967.
    • (1967) Proc. Natl. Acad. Sei. U.S.A. , vol.58 , pp. 1235
    • Taniuchi, H.1    Anfinsen, C.B.2    Sodja, A.3
  • 353
    • 0014430033 scopus 로고
    • Steps in the formation of active derivatives of staphylococcal nuclease during trypsin digestion
    • Taniuchi, H. and Anfinsen, C. B., Steps in the formation of active derivatives of staphylococcal nuclease during trypsin digestion, J. Biol. Chem., 243, 4778. 1968.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4778
    • Taniuchi, H.1    Anfinsen, C.B.2
  • 354
    • 0019088998 scopus 로고
    • Enzyme-catalyzed formation of semisynthetic staphylococcal nuclease using a new synthetic fragment, (48-Glycine) synthetic-(6-49)
    • Komoriya, A., Homandberg, G. A., and Chaiken, I. M., Enzyme-catalyzed formation of semisynthetic staphylococcal nuclease using a new synthetic fragment, (48-Glycine) synthetic-(6-49), hit. J. Peptide Protein. Res., 16, 433, 1980.
    • (1980) Hit. J. Peptide Protein. Res. , vol.16 , pp. 433
    • Komoriya, A.1    Homandberg, G.A.2    Chaiken, I.M.3
  • 356
    • 36949092676 scopus 로고
    • Amino-acid sequence of horse heart cytochrome c. The complete amino-acid sequence
    • Margoliash, E., Smith, E. L., Kreil, G., and Tuppy, H., Amino-acid sequence of horse heart cytochrome c. The complete amino-acid sequence. Nature (London),192, 1125, 1961.
    • (1961) Nature (London) , vol.192 , pp. 1125
    • Margoliash, E.1    Smith, E.L.2    Kreil, G.3    Tuppy, H.4
  • 357
    • 0017596122 scopus 로고
    • A functioning complex between tryptic fragments of cytochrome c. A route to the production of semisynthetic analogues
    • Harris, D. E. and OfTord, R. E., A functioning complex between tryptic fragments of cytochrome c. A route to the production of semisynthetic analogues, Biochem. J., 161, 21. 1977.
    • (1977) Biochem. J. , vol.161 , pp. 21
    • Harris, D.E.1    Oftord, R.E.2
  • 358
    • 84981626537 scopus 로고
    • Enzymatic synthesis of a peptide bond betweer a tryptic fragment of horse heart cytochrome c and a synthetic model peptide
    • Wcsterhuis, L. W., Tesser, G. I., and Nivard, R. J. F., Enzymatic synthesis of a peptide bond betweer a tryptic fragment of horse heart cytochrome c and a synthetic model peptide. Reel. Trav. Chim. Paxs-Bas,99, 400, 1980.
    • (1980) Reel. Trav. Chim. Paxs-Bas , vol.99 , pp. 400
    • Wcsterhuis, L.W.1    Tesser, G.I.2    Nivard, R.J.F.3
  • 359
    • 0019630048 scopus 로고
    • Clostripain-catalyzed re-formation of a peptide bond in a cyto chrome c fragment complex
    • Juillerat, M. and Homandberg, G. A., Clostripain-catalyzed re-formation of a peptide bond in a cyto chrome c fragment complex. Int. J. Peptide Protein Res., 18, 335, 1981.
    • (1981) Int. J. Peptide Protein Res. , vol.18 , pp. 335
    • Juillerat, M.1    Homandberg, G.A.2
  • 360
    • 85054369171 scopus 로고
    • Cytochrome c semisynthesis using enzymic resynthesi techniques
    • Blaha, K. and Malon, P. Eds., Walter di Gruyter, Berlin
    • Proudfoot, A. E. I. and Wallace, C. J. A., Cytochrome c semisynthesis using enzymic resynthesi techniques, in Peptides 1982, Proc. 17th Eur. Peptide Symp., Blaha, K. and Malon, P. Eds., Walter di Gruyter, Berlin, 1983, 353.
    • (1983) Peptides 1982, Proc. 17Th Eur. Peptide Symp , pp. 353
    • Proudfoot, A.E.I.1    Wallace, C.J.A.2
  • 361
    • 0343173486 scopus 로고
    • Human somatotropin: Covalent reconstitution of two polypeptide contiguou fragments with thrombin
    • Graf, L. and Li, C. H., Human somatotropin: covalent reconstitution of two polypeptide contiguou fragments with thrombin, Proc. Natl. Acad. Sci. U.S.A., 78, 6135, 1981.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6135
    • Graf, L.1    Li, C.H.2
  • 362
    • 0020490306 scopus 로고
    • Trypsin-catalyzed synthesis of peptide bond ii human hemoglobin. Oxygen binding characteristics of Gly-NH,(142a)Hb
    • Nagai, K., Enoki, Y., Tomita, S., and Teshima, T., Trypsin-catalyzed synthesis of peptide bond ii human hemoglobin. Oxygen binding characteristics of Gly-NH,(142a)Hb. J. Biol. Chem., 257, 1622, 1982
    • (1982) J. Biol. Chem. , vol.257 , pp. 1622
    • Nagai, K.1    Enoki, Y.2    Tomita, S.3    Teshima, T.4
  • 363
    • 0018572809 scopus 로고
    • X-ray diffraction and solution studie of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen linked chloride binding site at valine 1 a
    • O’Donnell, S., Mandaro, R., Schuster, T. M., and Arnone, A., X-ray diffraction and solution studie of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen linked chloride binding site at valine 1 a, J. Biol. Chem., 254, 12204, 1979.
    • (1979) J. Biol. Chem. , vol.254 , Issue.1 , pp. 2204
    • O’Donnell, S.1    Mandaro, R.2    Schuster, T.M.3    Arnone, A.4
  • 364
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 365
    • 0039233236 scopus 로고
    • Kinetics of the chymotrypsin-catalyzed condensation of A'-Benzoyl-L-tyrosine with glycylanilide
    • Gawron, O., Glaid, A. J., III, Boyle, R. E., and Odstrchel, G., Kinetics of the chymotrypsin-catalyzed condensation of A'-Benzoyl-L-tyrosine with glycylanilide. Arch. Biochem. Biophys., 95, 203, 1961.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 203
    • Gawron, O.1    Glaid, A.J.2    Boyle, R.E.3    Odstrchel, G.4
  • 366
    • 0343889591 scopus 로고
    • Some synthetic and hydrolytic experiments with chymotrypsin
    • Bergmann, M. and Fruton, J. S., Some synthetic and hydrolytic experiments with chymotrypsin, J. Biol. Chem., 124, 312, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 312
    • Bergmann, M.1    Fruton, J.S.2
  • 367
    • 0021761374 scopus 로고
    • Nucleophile specificity in chyniotrypsin peptide synthesis
    • Petkov, D. D. and Stoineva, I. B., Nucleophile specificity in chyniotrypsin peptide synthesis, Biochem. Biophys. Res. Commun., 118, 317. 1984.
    • (1984) Biochem. Biophys. Res. Commun. , vol.118 , pp. 317
    • Petkov, D.D.1    Stoineva, I.B.2
  • 368
    • 0021273238 scopus 로고
    • Kinetic studies on the mechanism and specificity of peptide synthesis catalyzed by thejerine proteases a-chymotrypsin and β-trypsin
    • Riechmann, L. and Kasche, V., Kinetic studies on the mechanism and specificity of peptide synthesis catalyzed by thejerine proteases a-chymotrypsin and β-trypsin, Biochem. Biophys. Res. Commun., 120, 686. 1984.
    • (1984) Biochem. Biophys. Res. Commun , vol.120 , pp. 686
    • Riechmann, L.1    Kasche, V.2
  • 369
    • 0021984633 scopus 로고
    • Peptide synthesis catalyzed by the serine proteinases chymotrypsin and trypsin
    • Riechmann, L. and Kasche, V., Peptide synthesis catalyzed by the serine proteinases chymotrypsin and trypsin, Biochim. Biophys. Acta,830, 164, 1985.
    • (1985) Biochim. Biophys. Acta , vol.830 , pp. 164
    • Riechmann, L.1    Kasche, V.2
  • 370
  • 371
    • 37049093939 scopus 로고
    • On the mechanism of the action of thermolysin: Kinetic study of the thermolysin-catalyzed condensation reaction of /V-Benzyloxycarbonyl-L-aspartic acid with L-phenylalanine methyl ester
    • Oyama, K., Kihara, K.-I., and Nonaka, Y., On the mechanism of the action of thermolysin: kinetic study of the thermolysin-catalyzed condensation reaction of /V-Benzyloxycarbonyl-L-aspartic acid with L-phenylalanine methyl ester, J. Chem. Soc. Perkin Trans., 2, 356, 1981.
    • (1981) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 356
    • Oyama, K.1    Kihara, K.-I.2    Nonaka, Y.3
  • 373
  • 374
    • 0020651938 scopus 로고
    • Thermodynamics and kinetics of the hydrolysis and resynthesis of the reactive site peptide bond in turkey ovomucoid third domain by aspergillopeptidase B
    • Ardelt, W. and Laskowski, M., Jr., Thermodynamics and kinetics of the hydrolysis and resynthesis of the reactive site peptide bond in turkey ovomucoid third domain by aspergillopeptidase B, Acta Biochim. Polonica,30, 115, 1983.
    • (1983) Acta Biochim. Polonica , vol.30 , pp. 115
    • Ardelt, W.1    Laskowski, M.2
  • 375
    • 0018099486 scopus 로고
    • Kinetics of the interaction of a-chymotrypsin with trypsin kallikrein inhibitor (Kunitz) in which the reactive-site peptide bond Lys-15— Ala-16 is split
    • Quast, U., Engel, J., Steffen, E., Tschesche, H., and Kupfer, S., Kinetics of the interaction of a-chymotrypsin with trypsin kallikrein inhibitor (Kunitz) in which the reactive-site peptide bond Lys-15— Ala-16 is split, Eur. J. Biochem., 86, 353, 1978.
    • (1978) Eur. J. Biochem. , vol.86 , pp. 353
    • Quast, U.1    Engel, J.2    Steffen, E.3    Tschesche, H.4    Kupfer, S.5
  • 376
    • 0019319066 scopus 로고
    • Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1
    • Estell, D. A., Wilson, K. A., and Laskowski, M., Jr., Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1, Biochemistry,19, 131, 1980.
    • (1980) Biochemistry , vol.19 , pp. 131
    • Estell, D.A.1    Wilson, K.A.2    Laskowski, M.3
  • 377
    • 0015849546 scopus 로고
    • PH dependence of the equilibrium constant for the hydrolysis of the ArgM-Ile reactive-site peptide bond in soybean trypsin inhibitor (Kunitz)
    • M-Ile reactive-site peptide bond in soybean trypsin inhibitor (Kunitz), Biochemistry,12, 2239, 1973.
    • (1973) Biochemistry , vol.12 , pp. 2239
    • Mattis, J.A.1    Laskowski, M.2
  • 378
    • 84954586137 scopus 로고
    • Kinetics of tryptic transpeptidation of insulins
    • Hruby, V. and Rich, D. H., Eds., Pierce Chem., Rockford
    • Markussen, J. and Volund, A., Kinetics of tryptic transpeptidation of insulins, in Proc. 8th Am. Peptide Symp., Hruby, V. and Rich, D. H., Eds., Pierce Chem., Rockford, 3., 1984, 207.
    • (1984) Proc. 8Th Am. Peptide Symp , vol.3 , pp. 207
    • Markussen, J.1    Volund, A.2
  • 379
    • 0021943042 scopus 로고
    • Kinetics of trypsin catalysis in the industrial conversion of porcine insulir to human insulin
    • Symp. Ill, Porter, R. and Clark, S., Eds., Ciba Foundation, Pitman, London
    • Markussen, J. and Volund, A., Kinetics of trypsin catalysis in the industrial conversion of porcine insulir to human insulin, in Enzymes in Organic Synthesis, Symp. Ill, Porter, R. and Clark, S., Eds., Ciba Foundation, Pitman, London, 1985, 188.
    • (1985) Enzymes in Organic Synthesis , pp. 188
    • Markussen, J.1    Volund, A.2
  • 380
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver, H. and Burk, D., The determination of enzyme dissociation constants, J. Am. Chem. Soc., 56, 658, 1934.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658
    • Lineweaver, H.1    Burk, D.2
  • 381
    • 0018635513 scopus 로고
    • Enzymatic synthesis of Leu- and Met-enkaphalin
    • Kullmann, W., Enzymatic synthesis of Leu- and Met-enkaphalin, Biochem. Biophys. Res. Commun., 91, 693, 1979.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 693
    • Kullmann, W.1
  • 382
    • 0019203667 scopus 로고
    • Proteases as catalysts of enzymic syntheses of opioid peptides
    • Kullmann, W., Proteases as catalysts of enzymic syntheses of opioid peptides, J. Biol. Chem., 255, 8234, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8234
    • Kullmann, W.1
  • 383
    • 0021247677 scopus 로고
    • Kinetics of chymotrypsin- and papain-catalyzed synthesis of (Leucine)enkephalin and (methionine)enkephalin
    • Kullmann, W., Kinetics of chymotrypsin- and papain-catalyzed synthesis of (leucine)enkephalin and (methionine)enkephalin, Biochem. J., 220, 405, 1984.
    • (1984) Biochem. J. , vol.220 , pp. 405
    • Kullmann, W.1
  • 384
    • 0004135644 scopus 로고
    • Freeman, Cooper and Co., San Francisco
    • Walsh, C., Enzymatic Reaction Mechanisms, Freeman, Cooper and Co., San Francisco, 1979, 53.
    • (1979) Enzymatic Reaction Mechanisms , pp. 53
    • Walsh, C.1
  • 385
    • 0015885480 scopus 로고
    • Enzymic mechanims involving concomitant transfer and hydrolysis reactions
    • Frère, J. M., Enzymic mechanims involving concomitant transfer and hydrolysis reactions, Biochem. J., 135, 469, 1973.
    • (1973) Biochem. J. , vol.135 , pp. 469
    • Frère, J.M.1
  • 386
    • 0014670232 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase
    • Folk, J. E., Mechanism of action of guinea pig liver transglutaminase, J. Biol. Chem., 244, 3707, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3707
    • Folk, J.E.1
  • 387
    • 50549188738 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: Nomenclature and theory
    • Cleland, W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory, Biochim. Biophys. Acta,67, 173, 1963.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 173
    • Cleland, W.W.1
  • 388
    • 50549204532 scopus 로고
    • The use of alternative substrates in studying enzymic mechanisms involving two substrates
    • Fromm, H. J., The use of alternative substrates in studying enzymic mechanisms involving two substrates. Biochim. Biophys. Acta,81. 413, 1964.
    • (1964) Biochim. Biophys. Acta , vol.81 , pp. 413
    • Fromm, H.J.1
  • 389
    • 85054414467 scopus 로고
    • Kleinzeller, A., Springer, G. P., and Wittmann, H. G., Eds., Springer-Verlag, Berlin
    • Fromm, H. J., Initial rate enzyme kinetics, in Molecular Biology, Biochemistry, and Biophysics, Vol. 22, Kleinzeller, A., Springer, G. P., and Wittmann, H. G., Eds., Springer-Verlag, Berlin, 1975, 152.
    • (1975) Molecular Biology, Biochemistry, and Biophysics , vol.22 , pp. 152
    • Fromm, H.J.1
  • 390
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York
    • Segel, I. W., Enzyme Kinetics, John Wiley and Sons, New York, 1975, 793.
    • (1975) Enzyme Kinetics , pp. 793
    • Segel, I.W.1
  • 391
    • 0014405092 scopus 로고
    • On the active site of proteascs. III. Mapping the active site of papain; specific peptide inhibitors of papain
    • Schechter, I. and Berger, A., On the active site of proteascs. III. Mapping the active site of papain; specific peptide inhibitors of papain, Biochem. Biophys. Res. Commun.32, 898, 1968.
    • (1968) Biochem. Biophys. Res. Commun. , vol.32 , pp. 898
    • Schechter, I.1    Berger, A.2
  • 394
    • 0001473269 scopus 로고
    • Enzymatic removal of the protecting group in peptide synthesis
    • Holley, R. W., Enzymatic removal of the protecting group in peptide synthesis, J. Am. Chem. Soc., 77, 2552, 1955.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 2552
    • Holley, R.W.1
  • 395
    • 0016691151 scopus 로고
    • Enzymes as reagents in peptide synthesis: Enzymatic removal of amine protecting groups
    • Meyers, C. and Glass, J. D., Enzymes as reagents in peptide synthesis: enzymatic removal of amine protecting groups, Proc. Natl. Acad. Sei. U.S.A., 72, 2193, 1975.
    • (1975) Proc. Natl. Acad. Sei. U.S.A. , vol.72 , pp. 2193
    • Meyers, C.1    Glass, J.D.2
  • 396
    • 0019369289 scopus 로고
    • Enzymes as reagents in the synthesis of peptides
    • Glass, J. D., Enzymes as reagents in the synthesis of peptides. Enzyme Microb. Technol., 3, 2, 1981.
    • (1981) Enzyme Microb. Technol. , vol.3 , pp. 2
    • Glass, J.D.1
  • 397
    • 0013650974 scopus 로고
    • Use of proteolytic enzymes for synthesis of fragments of mouse epidermal growth factor
    • Regnarsson. U. Ed., Almquist and Wiksell International. Stockholm
    • Widmer, F., Bayne, S., Houen, G., Moss, B. A., Rigby, R. D., Whittacker, R. G., and Johansen, J. T., Use of proteolytic enzymes for synthesis of fragments of mouse epidermal growth factor, in Peptides 1984, Proc. 18th Eur. Peptide Symp., Regnarsson. U. Ed., Almquist and Wiksell International. Stockholm. 1984. 193.
    • (1984) Peptides 1984, Proc. 18Th Eur. Peptide Symp , pp. 193
    • Widmer, F.1    Bayne, S.2    Houen, G.3    Moss, B.A.4    Rigby, R.D.5    Whittacker, R.G.6    Johansen, J.T.7
  • 398
    • 84914556676 scopus 로고
    • Carboxypeptidase Y as a catalyst for peptide synthesis in aqueous phase with minimal protection
    • Brunfeldt, K., Ed. Scriptor, Copenhagen
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y as a catalyst for peptide synthesis in aqueous phase with minimal protection, in Peptides 1980, Proc. 16th Eur. Peptide Symp., Brunfeldt, K., Ed. Scriptor, Copenhagen, 1981, 46.
    • (1981) Peptides 1980, Proc. 16Th Eur. Peptide Symp , pp. 46
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 400
    • 0003065770 scopus 로고
    • Properties of the penicillin deacylase enzyme of
    • Cole, M., Properties of the penicillin deacylase enzyme ofEscherichia coli. Nature (London),203, 519, 1964.
    • (1964) Escherichia Coli. Nature (London) , vol.203 , pp. 519
    • Cole, M.1
  • 401
    • 0006387991 scopus 로고
    • Variety of substrates for a bacterial benzyl penicillin-splitting enzyme
    • Kaufmann, W. and Bauer, K., Variety of substrates for a bacterial benzyl penicillin-splitting enzyme. Nature (London),203, 520, 1964.
    • (1964) Nature (London) , vol.203 , pp. 520
    • Kaufmann, W.1    Bauer, K.2
  • 402
    • 85054400710 scopus 로고
    • Use of phenacetyl group for protection of the lysine N*-amino group in synthesis of peptides
    • Brtnik, F., Barth, T., and Jost, K., Use of phenacetyl group for protection of the lysine N*-amino group in synthesis of peptides, Collect. Czech. Chem. Commun.46, 1983, 1981.
    • (1983) Collect. Czech. Chem. Commun , vol.46 , pp. 1981
    • Brtnik, F.1    Barth, T.2    Jost, K.3
  • 403
    • 84958056764 scopus 로고
    • The specific peptidase and esterase activities of Chymotrypsin, Arch
    • Kaufman, S., Schwert, G. W., and Neurath, H., The specific peptidase and esterase activities of Chymotrypsin, Arch. Biochem., 17, 203, 1948.
    • (1948) Biochem. , vol.17 , pp. 203
    • Kaufman, S.1    Schwert, G.W.2    Neurath, H.3
  • 405
    • 0006711618 scopus 로고
    • The kinetics of the amidase and esterase activities of trypsin
    • Schwert, G. W. and Eisenberg, M. A., The kinetics of the amidase and esterase activities of trypsin, J. Biol. Chem., 179, 665, 1949.
    • (1949) J. Biol. Chem. , vol.179 , pp. 665
    • Schwert, G.W.1    Eisenberg, M.A.2
  • 406
    • 0000437125 scopus 로고
    • Peptide synthesis. An application of the esterase activity of Chymotrypsin
    • Walton, E., Rodin, J. O., Stammer, C. H., and Holly, F. W., Peptide synthesis. An application of the esterase activity of Chymotrypsin. J. Org. Chem., 27, 2255, 1962.
    • (1962) J. Org. Chem. , vol.27 , pp. 2255
    • Walton, E.1    Rodin, J.O.2    Stammer, C.H.3    Holly, F.W.4
  • 408
    • 85004788908 scopus 로고
    • Verwendung von alkalischer Protease des Bacillus-subtilis-Stammes DY zur Hydrolyse von Aminosäuve und PeptidEstern, Hoppe-Seyler’s Z
    • Alekslev, B., Schamilian, P., Widenow, G., Stoev, S., Zachariev, S., Golovinsky, E., Verwendung von alkalischer Protease des Bacillus-subtilis-Stammes DY zur Hydrolyse von Aminosäuve und PeptidEstern, Hoppe-Seyler’s Z. Physiol.Chem., 362, 1323, 1981.
    • (1981) Physiol.Chem. , vol.362 , pp. 1323
    • Alekslev, B.1    Schamilian, P.2    Widenow, G.3    Stoev, S.4    Zachariev, S.5    Golovinsky, E.6
  • 409
    • 85054365350 scopus 로고
    • Thermitase-catalyzed hydrolysis of the C-terminal ester group of protected peptide ester derivatives
    • Blahâ, K. and Malon, P. Eds., Walter de Gruyter, Berlin
    • Hermann, P. and Salewski, L., Thermitase-catalyzed hydrolysis of the C-terminal ester group of protected peptide ester derivatives, in Peptides 1982, Proc. 17th Eur. Peptide Symp., Blahâ, K. and Malon, P. Eds., Walter de Gruyter, Berlin. 1983, 39.
    • (1983) Peptides 1982, Proc. 17Th Eur. Peptide Symp , pp. 39
    • Hermann, P.1    Salewski, L.2
  • 410
    • 33845559077 scopus 로고
    • Peptide synthesis in water and the use of immobilized carboxipeptidase Y for deprotection
    • Royer, G. P. and Anantharamaiah, G. M., Peptide synthesis in water and the use of immobilized carboxipeptidase Y for deprotection, J. Am. Chem. Soc., 101, 3394, 1979.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3394
    • Royer, G.P.1    Anantharamaiah, G.M.2
  • 411
    • 0018886958 scopus 로고
    • Use of immobilized carboxypeptidase Y (I- CPY) as a catalyst for deblocking in peptide synthesis
    • Royer, G. P., Hsiao, H. Y., and Anantharamaiah, G. M., Use of immobilized carboxypeptidase Y (I- CPY) as a catalyst for deblocking in peptide synthesis, Biochemie, 62, 537, 1980.
    • (1980) Biochemie , vol.62 , pp. 537
    • Royer, G.P.1    Hsiao, H.Y.2    Anantharamaiah, G.M.3
  • 412
    • 0001120111 scopus 로고
    • Eine neue Methode zur Synthese von Polypeptiden
    • Mutter, M., Hagenmaier, H., and Bayer, E., Eine neue Methode zur Synthese von Polypeptiden, Angew. Chem., 83, 883, 1971.
    • (1971) Angew. Chem. , vol.83 , pp. 883
    • Mutter, M.1    Hagenmaier, H.2    Bayer, E.3
  • 413
    • 84981433983 scopus 로고
    • Peptidsynthesen in wäsSr.Iger Phase. I. Polyäthylenimin als wasserlöslicher Träger bei der A-carboxyanhydrid-Methode
    • Blecher, H. and Pfaender, P., Peptidsynthesen in wäsSr.iger Phase. I. Polyäthylenimin als wasserlöslicher Träger bei der A'-carboxyanhydrid-Methode, Justus Liebigs Atm. Chem., 1263, 1973.
    • (1973) Justus Liebigs Atm. Chem , pp. 1263
    • Blecher, H.1    Pfaender, P.2
  • 414
    • 0014823488 scopus 로고
    • Partial enzymic deprotection in the synthesis of a protected octapeptide bearing a free terminal carboxyl group
    • Ohno, M. and Anfinsen, C. B., Partial enzymic deprotection in the synthesis of a protected octapeptide bearing a free terminal carboxyl group, J. Am. Chem. Soc., 92, 4098, 1970.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 4098
    • Ohno, M.1    Anfinsen, C.B.2
  • 415
    • 0014393907 scopus 로고
    • Characterization of Staphylococcal nuclease and the status of studies on its chemical synthesis
    • Anfinsen, C. B., Characterization of Staphylococcal nuclease and the status of studies on its chemical synthesis, Pure Appl. Chem., 17, 461, 1968.
    • (1968) Pure Appl. Chem. , vol.17 , pp. 461
    • Anfinsen, C.B.1
  • 416
    • 84985657615 scopus 로고
    • Reversal of enzymatic hydrolysis: Rate and extent of ester synthesis as catalyzed by Chymotrypsin and subtilisin Carlsberg at low water concentrations
    • Ingalls, R. G., Squires, R. G., and Butler, L. G., Reversal of enzymatic hydrolysis: rate and extent of ester synthesis as catalyzed by Chymotrypsin and subtilisin Carlsberg at low water concentrations, Biotechnol. Bioeng., 17, 1627, 1975.
    • (1975) Biotechnol. Bioeng. , vol.17 , pp. 1627
    • Ingalls, R.G.1    Squires, R.G.2    Butler, L.G.3
  • 417
    • 0019879061 scopus 로고
    • Enzymatic synthesis in biphasic aqueous organic systems. I. Chemical equilibrium shift
    • Martinek, K., Semenov, A. N., and Berezin, I. V., Enzymatic synthesis in biphasic aqueous organic systems. I. Chemical equilibrium shift, Biochim. Biophys. Acta,658, 76, 1981.
    • (1981) Biochim. Biophys. Acta , vol.658 , pp. 76
    • Martinek, K.1    Semenov, A.N.2    Berezin, I.V.3
  • 418
    • 84910330723 scopus 로고
    • Synthèse enzymatique d’esters d’acides aminés en milieu organique
    • Tarquis, D., Monsan, P., and Durand, G., Synthèse enzymatique d’esters d’acides aminés en milieu organique, Bull. Soc. Chim. Fr., 2, 76, 1980.
    • (1980) Bull. Soc. Chim. Fr. , vol.2 , pp. 76
    • Tarquis, D.1    Monsan, P.2    Durand, G.3
  • 419
    • 0343167841 scopus 로고
    • Optimization of the enzymatic synthesis of amino acid esters. Reaction in polyphasic medium
    • Vidaluc, J. L., Baboulene, M., Speziale, V., Lattes, A., and Monsan, P., Optimization of the enzymatic synthesis of amino acid esters. Reaction in polyphasic medium. Tetrahedron,39, 269, 1983.
    • (1983) Tetrahedron , pp. 269
    • Vidaluc, J.L.1    Baboulene, M.2    Speziale, V.3    Lattes, A.4    Monsan, P.5
  • 421
    • 0002918033 scopus 로고
    • The enzymatic synthesis of peptide bonds
    • Bergmann, M. and Fraenkel-Conrat, H., The enzymatic synthesis of peptide bonds, J. Biol. Chem., 124, 1, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 1
    • Bergmann, M.1    Fraenkel-Conrat, H.2
  • 422
    • 0343889591 scopus 로고
    • Some synthetic and hydrolytic experiments with chymotrypsin
    • Bergmann, M. and Fruton, J. S., Some synthetic and hydrolytic experiments with chymotrypsin, J. Biol. Chem., 124, 321, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 321
    • Bergmann, M.1    Fruton, J.S.2
  • 423
    • 76549257455 scopus 로고
    • Enzymatic synthesis of peptide bonds. II. “Preferences” of papain within the monoaminomonocarboxylic acid series
    • Fox, S. W., Pettinga, C. W., Halverson, J. S., and Wax, H., Enzymatic synthesis of peptide bonds. II. “Preferences” of papain within the monoaminomonocarboxylic acid series, Arch. Biochem., 25, 21, 1950.
    • (1950) Arch. Biochem. , vol.25 , pp. 21
    • Fox, S.W.1    Pettinga, C.W.2    Halverson, J.S.3    Wax, H.4
  • 424
    • 50549195940 scopus 로고
    • The papain-catalyzed synthesis of hippuryl anilide 1. General properties of the enzyme system
    • Carty, R. P. and Kirschenbaum, D. M., The papain-catalyzed synthesis of hippuryl anilide 1. General properties of the enzyme system, Biochim. Biophys. Acta,85, 446. 1964.
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 446
    • Carty, R.P.1    Kirschenbaum, D.M.2
  • 425
    • 0000338208 scopus 로고
    • The role of specificity in the enzymatic synthesis of proteins. Syntheses with intracellular enzymes
    • Bergmann, M. and Fraenkel-Conrat, H., The role of specificity in the enzymatic synthesis of proteins. Syntheses with intracellular enzymes, J. Biol. Chem., 119, 707, 1937.
    • (1937) J. Biol. Chem. , vol.119 , pp. 707
    • Bergmann, M.1    Fraenkel-Conrat, H.2
  • 426
    • 2142822422 scopus 로고
    • The oxidative cleavage of phenylhydrazide groups from carboallyloxy-a-amino acid phenylhydrazides and carboallyloxydipeptide phenylhydrazides
    • Milne, H. B., Halver, J. E., Ho, D. S., and Mason, M. S., The oxidative cleavage of phenylhydrazide groups from carboallyloxy-a-amino acid phenylhydrazides and carboallyloxydipeptide phenylhydrazides, J. Am. Chem. Soc., 79, 637, 1957.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 637
    • Milne, H.B.1    Halver, J.2    Ho, E.D.S.3    Mason, M.S.4
  • 427
    • 33947452112 scopus 로고
    • Amino acid derivatives. 11. Enzymatic synthesis of phenylhydrazides of carboallyloxyamino acids
    • Milne, B. H. and Stevens, C. M., Amino acid derivatives. 11. Enzymatic synthesis of phenylhydrazides of carboallyloxyamino acids, J. Am. Chem. Soc., 72, 1742, 1950.
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 1742
    • Milne, B.H.1    Stevens, C.M.2
  • 428
    • 0014397138 scopus 로고
    • Peptide synthesis via oxidation of iV-acyl-a-amino acid phenylhydrazides. III. Dialanyl-insulin and diphenylalanyl-insulin
    • Milne, B. H. and Carpenter, F. H., Peptide synthesis via oxidation of iV-acyl-a-amino acid phenylhydrazides. III. Dialanyl-insulin and diphenylalanyl-insulin, J. Org. Chem., 33, 4476, 1968.
    • (1968) J. Org. Chem. , vol.33 , pp. 4476
    • Milne, B.H.1    Carpenter, F.H.2
  • 429
    • 0019203667 scopus 로고
    • Proteases as catalysts for enzymic syntheses of opioid peptides
    • Kullmann, W., Proteases as catalysts for enzymic syntheses of opioid peptides, J. Biol. Chem.255, 8234, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8234
    • Kullmann, W.1
  • 430
    • 0012604455 scopus 로고
    • Protease-catalyzed peptide bond formation: Application to synthesis of the COOH-terminal octapeptide amide of cholecystokinin
    • Kullmann, W., Protease-catalyzed peptide bond formation: application to synthesis of the COOH-terminal octapeptide amide of cholecystokinin, Proc. Natl. Acad. Sci. U.S.A., 79, 2840, 1982.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 2840
    • Kullmann, W.1
  • 431
    • 84912864758 scopus 로고
    • Papain-catalyzed synthesis of phenylhydrazides of A-acyl amino acids
    • Cerovsky, V. and Jost, K., Papain-catalyzed synthesis of phenylhydrazides of A-acyl amino acids. Collect. Czech. Chem. Commun., 49, 2557, 1984.
    • (1984) Collect. Czech. Chem. Commun. , vol.49 , pp. 2557
    • Cerovsky, V.1    Jost, K.2
  • 432
    • 0020123473 scopus 로고
    • The proteinase-catalyzed synthesis of peptide hydrazides
    • Jones, R. M. L. and Offord, R. E., The proteinase-catalyzed synthesis of peptide hydrazides, Biochem. J., 203, 125, 1982.
    • (1982) Biochem. J. , vol.203 , pp. 125
    • Jones, R.M.L.1    Offord, R.E.2
  • 433
    • 0019531170 scopus 로고
    • Studies on protein semisynthesis. I. Formation of esters, hydrazides, and substituted hydrazides of peptides by the reverse reaction of trypsin
    • Yagisawa, S., Studies on protein semisynthesis. I. Formation of esters, hydrazides, and substituted hydrazides of peptides by the reverse reaction of trypsin, J. Biochem., 89, 491, 1981.
    • (1981) J. Biochem. , vol.89 , pp. 491
    • Yagisawa, S.1
  • 434
    • 0010561365 scopus 로고
    • Peptide synthesis via oxidation of A'-acetyl-a-amino acid phenylhydrazides
    • Milne, H. B. and Kilday, W., Peptide synthesis via oxidation of A'-acetyl-a-amino acid phenylhydrazides, J. Org. Chem., 30, 64, 1965.
    • (1965) J. Org. Chem. , vol.30 , pp. 64
    • Milne, H.B.1    Kilday, W.2
  • 435
    • 0019788208 scopus 로고
    • Semisynthesis of insulin: Specific activation of the arginine carboxyl group of the B chain of desoctapeptide-(B23-30)-insulin (bovine)
    • Canova-Davis, F. and Carpenter, F. H., Semisynthesis of insulin: specific activation of the arginine carboxyl group of the B chain of desoctapeptide-(B23-30)-insulin (bovine), Biochemistry,20, 7053, 1981.
    • (1981) Biochemistry , vol.20 , pp. 7053
    • Canova-Davis, F.1    Carpenter, F.H.2
  • 436
    • 0017379341 scopus 로고
    • Enzymes as reagents in peptide synthesis: Enzyme-labile protection for carboxyl groups
    • Glass, J. and Pelzig, M., Enzymes as reagents in peptide synthesis: enzyme-labile protection for carboxyl groups, Proc. Natl. Acad. Sci. U.S.A., 74, 2739, 1977.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2739
    • Glass, J.1    Pelzig, M.2
  • 437
    • 85054413704 scopus 로고
    • Purification and properties of a clostridiopeptidase B (Clostripain)
    • Mitchel, W. M. and Harrington, W. F., Purification and properties of a clostridiopeptidase B (clostripain), J. Biol. Chem., 23, 4683, 1980.
    • (1980) J. Biol. Chem. , vol.23 , pp. 4683
    • Mitchel, W.M.1    Harrington, W.F.2
  • 438
    • 0016280663 scopus 로고
    • Enzymatic cleavage of the N“-acetyl protecting group from lysine in proteins (Kunitz-trypsin-kallikrein-inhibitor) in vitro and in vivo
    • Jering, H., Schorp, G., and Tschesche, H., Enzymatic cleavage of the N“-acetyl protecting group from lysine in proteins (Kunitz-trypsin-kallikrein-inhibitor) in vitro and in vivo, Hoppe-Sexler'sZ. Phxsiol. Chem., 355, 1129, 1974.
    • (1974) Hoppe-Sexler'sz. Phxsiol. Chem. , vol.355 , pp. 1129
    • Jering, H.1    Schorp, G.2    Tschesche, H.3
  • 439
    • 84955355423 scopus 로고
    • Pyroglutamyl groups as enzyme-labile protection of the lysine side-chain
    • Hruby, V. and Rich, D. H., Eds., Pierce Chemical, Rockford
    • Glass, J. D. and Pande, C. S., Pyroglutamyl groups as enzyme-labile protection of the lysine side-chain, in Peptides — Structure and Function, Proc. 8th Am. Peptide Symp., Hruby, V. and Rich, D. H., Eds., Pierce Chemical, Rockford, 3., 1984, 203.
    • (1984) Peptides — Structure and Function, Proc. 8Th Am. Peptide Symp , vol.3 , pp. 203
    • Glass, J.D.1    Pande, C.S.2
  • 440
    • 0002918033 scopus 로고
    • The enzymatic synthesis of peptide bonds
    • Bergmann, M. and Fraenkel-Conrat, H., The enzymatic synthesis of peptide bonds, J. Biol. Chem., 124, 1, 1938.
    • (1938) J. Biol. Chem. , vol.124 , pp. 1
    • Bergmann, M.1    Fraenkel-Conrat, H.2
  • 441
    • 33947458917 scopus 로고
    • Enzymic synthesis of peptide bonds. V. Instances of proteasecontrolled specificity in the synthesis of acylamino acid anilides and acylpeptide anilides
    • Janssen, F., Winitz, M., and Fox, S. W., Enzymic synthesis of peptide bonds. V. Instances of proteasecontrolled specificity in the synthesis of acylamino acid anilides and acylpeptide anilides, J. Am. Chem. Soc., 75, 704, 1953.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 704
    • Janssen, F.1    Winitz, M.2    Fox, S.W.3
  • 442
    • 0014240848 scopus 로고
    • Peptide synthesis via oxidation of A'-acyl-a-amino acid phenylhy-drazides. II. Benzyloxycarbonyl peptide phenylhydrazides
    • Milne, B. H. and Most, Jr., C. F., Peptide synthesis via oxidation of A'-acyl-a-amino acid phenylhy-drazides. II. Benzyloxycarbonyl peptide phenylhydrazides, J. Org. Chem., 33, 169, 1968.
    • (1968) J. Org. Chem. , vol.33 , pp. 169
    • Milne, B.H.1    Most, C.F.2
  • 443
    • 0019467848 scopus 로고
    • Protease-mediated peptide bond formation. On some unexpected outcomes during enzymatic synthesis of Leu-enkephalin
    • Kullmann, W., Protease-mediated peptide bond formation. On some unexpected outcomes during enzymatic synthesis of Leu-enkephalin, J. Biol. Chem., 256, 1301, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1301
    • Kullmann, W.1
  • 444
    • 0018883726 scopus 로고
    • Trypsin-catalyzed conversion of Staphylococcal nuclease-T fragment complexes to covalent forms
    • Homandberg, G. A. and Chaiken, I. M., Trypsin-catalyzed conversion of Staphylococcal nuclease-T fragment complexes to covalent forms, J. Biol. Chem., 255, 4903, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4903
    • Homandberg, G.A.1    Chaiken, I.M.2
  • 445
    • 0011300588 scopus 로고
    • Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis
    • Breddam, K., Widmer, F., and Johansen, J. T., Carboxypeptidase Y catalyzed transpeptidations and enzymatic peptide synthesis, Carlsberg Res. Commun., 45, 237, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 237
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 446
    • 0000990957 scopus 로고
    • Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y catalyzed peptide synthesis using amino acid alkyl esters as amine components, Carlsberg Res. Commun., 45, 453, 1980.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 453
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 447
    • 84914556676 scopus 로고
    • Carboxypeptidase Y as a catalyst for peptide synthesis in aqueous phase with minimal protection
    • Brunfeldt, K., Ed., Scriptor, Copenhagen
    • Widmer, F., Breddam, K., and Johansen, J. T., Carboxypeptidase Y as a catalyst for peptide synthesis in aqueous phase with minimal protection, in Peptides 1980, Proc. 16th Eur. Peptide Symp., Brunfeldt, K., Ed., Scriptor, Copenhagen, 1981, 46.
    • (1981) Peptides 1980, Proc. 16Th Eur. Peptide Symp , pp. 46
    • Widmer, F.1    Breddam, K.2    Johansen, J.T.3
  • 448
    • 3142578831 scopus 로고
    • Carboxypeptidase Y catalyzed C-terminal modification in the B-chain of porcine insulin
    • Breddam, K., Widmer, F., and Johansen, J. T., Carboxypeptidase Y catalyzed C-terminal modification in the B-chain of porcine insulin, Carlsberg Res. Commun., 46, 361, 1981.
    • (1981) Carlsberg Res. Commun. , vol.46 , pp. 361
    • Breddam, K.1    Widmer, F.2    Johansen, J.T.3
  • 449
    • 84948319743 scopus 로고
    • Monitoring of protease-catalyzed peptide synthesis by high performance liquid chromatography
    • Kullmann, W., Monitoring of protease-catalyzed peptide synthesis by high performance liquid chromatography, J. Liquid Chromatog., 4, 1121, 1981.
    • (1981) J. Liquid Chromatog. , vol.4 , pp. 1121
    • Kullmann, W.1
  • 450
    • 0019203667 scopus 로고
    • Proteases as catalysts for enzymic syntheses of opioid peptides
    • Kullmann, W., Proteases as catalysts for enzymic syntheses of opioid peptides, J. Biol. Chem., 255, 8234, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8234
    • Kullmann, W.1
  • 451
    • 0019709643 scopus 로고
    • Rapid characterization by thin-layer chromatography of amino acid and peptide derivatives enzymically prepared during protease-mediated peptide synthesis
    • Kullmann, W., Rapid characterization by thin-layer chromatography of amino acid and peptide derivatives enzymically prepared during protease-mediated peptide synthesis, J. Liquid Chromatog., 4, 1947, 1981.
    • (1981) J. Liquid Chromatog. , vol.4 , pp. 1947
    • Kullmann, W.1
  • 452
    • 0020359083 scopus 로고
    • Enzymatic synthesis of dynorphinl 8
    • l 8, J. Org. Chem., 47, 5300, 1982.
    • (1982) J. Org. Chem. , vol.47 , pp. 5300
    • Kullmann, W.1
  • 453
    • 0012604455 scopus 로고
    • Protease-catalyzed peptide bond formation: Application to synthesis of the COOH-terminal octapeptide of cholecystokinin
    • Kullmann, W., Protease-catalyzed peptide bond formation: Application to synthesis of the COOH-terminal octapeptide of cholecystokinin, Proc. Natl. Acad. Sci. U.S.A., 79, 2840, 1982.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 2840
    • Kullmann, W.1
  • 454
    • 0021019341 scopus 로고
    • Protease-catalyzed synthesis of melanocyte-stimulating hormone (MSH) fragments
    • Kullmann, W., Protease-catalyzed synthesis of melanocyte-stimulating hormone (MSH) fragments, J. Protein Chem., 2, 289, 1983.
    • (1983) J. Protein Chem. , vol.2 , pp. 289
    • Kullmann, W.1
  • 455
    • 0021769528 scopus 로고
    • Reactions of the aminoacyl-tRNA synthetase-aminoacyl adenylate complex and amino acid derivatives. A new approach to peptide synthesis
    • Nakajima, H., Kitabatake, S., Tsurutani, R., Tomioka, I., Yamamoto, K., and Imahori, K., Reactions of the aminoacyl-tRNA synthetase-aminoacyl adenylate complex and amino acid derivatives. A new approach to peptide synthesis, Biochim. Biophys. Acta,790, 197, 1984.
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 197
    • Nakajima, H.1    Kitabatake, S.2    Tsurutani, R.3    Tomioka, I.4    Yamamoto, K.5    Imahori, K.6
  • 456
    • 0021767226 scopus 로고
    • Need a catalyst? Design an enzyme
    • Maugh, II, T. H., Need a catalyst? Design an enzyme, Science,223, 269, 1984.
    • (1984) Science , vol.223 , pp. 269
    • Maugh, T.H.1
  • 457
    • 0014023148 scopus 로고
    • Synthetic peptide models of enzyme active sites. III. Stereoselective esterase models
    • Sheehan, J. C., Bennett, G. B., and Schneider, J. A., Synthetic peptide models of enzyme active sites. III. Stereoselective esterase models, J. Am. Chem. Soc., 88, 3455, 1966.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 3455
    • Sheehan, J.C.1    Bennett, G.B.2    Schneider, J.A.3
  • 458
    • 0017177594 scopus 로고
    • Synthesis and catalytic properties of peptides with hydrolytic activity, Z. Naturforsch
    • Petz, D., and Schneider, F., Synthesis and catalytic properties of peptides with hydrolytic activity, Z. Naturforsch., 31c, 534, 1976.
    • (1976) 31C , pp. 534
    • Petz, D.1    Schneider, F.2
  • 459
    • 85054345256 scopus 로고
    • Synthesis of linear-, cyclic-, and poly-peptides having the sequence -Asp-eAhx-Ser-eAhx-His-eAhx-, and their ester hydrolytic reactions
    • S. Sakakibara, Ed., Protein Research Foundation, Osaka, Japan
    • Nakajima, B.-I. and Nishi, N., Synthesis of linear-, cyclic-, and poly-peptides having the sequence -Asp-eAhx-Ser-eAhx-His-eAhx-, and their ester hydrolytic reactions, in Peptide Chemistry 1982, S. Sakakibara, Ed., Protein Research Foundation, Osaka, Japan, 1983, 41.
    • (1983) Peptide Chemistry 1982 , pp. 41
    • Nakajima, B.-I.1    Nishi, N.2
  • 460
    • 0042313503 scopus 로고
    • An incremental approach to hosts that mimic serine proteases
    • Cram, D. J. and Katz, H. E., An incremental approach to hosts that mimic serine proteases, J. Am. Chem. Soc., 105, 135, 1983.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 135
    • Cram, D.J.1    Katz, H.E.2
  • 461
    • 33845552493 scopus 로고
    • Optimization of metallocene substrates for 3-cyclodextrin reactions
    • Breslow, R., Trainor, G., and Ucno, A., Optimization of metallocene substrates for 3-cyclodextrin reactions, J. Am. Chem. Soc., 105, 2739, 1983.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2739
    • Breslow, R.1    Trainor, G.2    Ucno, A.3
  • 463
    • 0037683935 scopus 로고
    • Hydrolysis of active esters of aliphatic carboxylic acids with cyclic dipeptide catalysts consisting of L-histidine and different aliphatic a-amino acids
    • Masuda, Y., Tanihara, M., Imanishi, Y., and Higashimura, T., Hydrolysis of active esters of aliphatic carboxylic acids with cyclic dipeptide catalysts consisting of L-histidine and different aliphatic a-amino acids, Bull. Chem. Soc. Jpn., 58, 497, 1985.
    • (1985) Bull. Chem. Soc. Jpn. , vol.58 , pp. 497
    • Masuda, Y.1    Tanihara, M.2    Imanishi, Y.3    Higashimura, T.4
  • 464
    • 1542584459 scopus 로고
    • Biomimetic models for cysteine proteases. II. Nucleophilic thiolate-containing zwitterions produced from imidazole-thiol pairs. A model of the acylation step in papain-mediated hydrolyses, i
    • Skorey, K. J. and Brown, R. S., Biomimetic models for cysteine proteases. II. Nucleophilic thiolate-containing zwitterions produced from imidazole-thiol pairs. A model of the acylation step in papain-mediated hydrolyses, i. Am. Chem. Soc., 107, 4070, 1985.
    • (1985) Am. Chem. Soc. , vol.107 , pp. 4070
    • Skorey, K.J.1    Brown, R.S.2
  • 466
    • 33845186193 scopus 로고
    • A protease mimic with turnover capabilities
    • Menger, F. M. and Whitesell, L. G., A protease mimic with turnover capabilities, J. Am. Chem. Soc., 107. 707, 1985.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 707
    • Menger, F.M.1    Whitesell, L.G.2
  • 467
    • 0001645404 scopus 로고
    • Functionalized crown ethers as an approach to the enzyme model for the synthesis of peptides
    • Sasaki, S., Shionoya, M., and Koga, K., Functionalized crown ethers as an approach to the enzyme model for the synthesis of peptides, J. Am. Chem. Soc., 107, 3371, 1985.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3371
    • Sasaki, S.1    Shionoya, M.2    Koga, K.3
  • 468
    • 0001423787 scopus 로고
    • Nonribosomal polypeptide synthesis on polyenzyme templates
    • Lipmann, F., Nonribosomal polypeptide synthesis on polyenzyme templates. Act. Chem. Res., 6, 361, 1973.
    • (1973) Act. Chem. Res. , vol.6 , pp. 361
    • Lipmann, F.1
  • 469
    • 0019508396 scopus 로고
    • Ribosomal components from Escherichia coli 50 S subunits involved in reconstitution of peptidyltransferase activity
    • Hampl, H., Schulze, H., and Nierhaus, K. H., Ribosomal components from Escherichia coli 50 S subunits involved in reconstitution of peptidyltransferase activity, J. Biol. Chem.256, 2284, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2284
    • Hampl, H.1    Schulze, H.2    Nierhaus, K.H.3
  • 471
    • 0020984194 scopus 로고
    • The design of biologically active polypeptides
    • Robson, B., The design of biologically active polypeptides, Crit. Rev. Biochem., 14, 273, 1984.
    • (1984) Crit. Rev. Biochem , vol.14 , pp. 273
    • Robson, B.1
  • 472
    • 33847799412 scopus 로고
    • Structure and mechanism of chymotrypsin
    • Blow, D. M., Structure and mechanism of chymotrypsin, Acc. Chem. Res.9, 145. 1976.
    • (1976) Acc. Chem. Res , vol.9 , pp. 145
    • Blow, D.M.1
  • 473
    • 0017784004 scopus 로고
    • A new amino protecting group removable by reduction. Chemistry of the dithiasuccinoyl (Dts) function
    • Barany, G. and Merrifield, R. B., A new amino protecting group removable by reduction. Chemistry of the dithiasuccinoyl (Dts) function, J. Am. Chem. Soc., 99, 7363, 1977.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 7363
    • Barany, G.1    Merrifield, R.B.2
  • 475
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 476
    • 0000636758 scopus 로고
    • Enzyme peptide synthesis by an iterative procedure in a nucleophile pool
    • Petkov, D. D. and Stoineva, I. B., Enzyme peptide synthesis by an iterative procedure in a nucleophile pool, Tetrahedron Lett., 25, 3751, 1984
    • (1984) Tetrahedron Lett. , vol.25 , pp. 3751
    • Petkov, D.D.1    Stoineva, I.B.2
  • 478
    • 0020012477 scopus 로고
    • Proteinase-catalyzed synthesis of peptide bonds
    • Fruton, J. S., Proteinase-catalyzed synthesis of peptide bonds. Adv. Enzymol. Relat. Areas Mol. Biol., 53, 239, 1982.
    • (1982) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.53 , pp. 239
    • Fruton, J.S.1
  • 479
    • 0019964097 scopus 로고
    • Proteasen als Biokatalysatoren für die Peptidsynthese
    • Jakubke, H.-D. and Kuhl, P., Proteasen als Biokatalysatoren für die Peptidsynthese, Pharmazie,37, 89, 1982.
    • (1982) Pharmazie , vol.37 , pp. 89
    • Jakubke, H.-D.1    Kuhl, P.2
  • 480
    • 0344520082 scopus 로고
    • Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung
    • Jakubke, H.-D., Kuhl, P. and Könnecke, A., Grundprinzipien der proteasekatalysierten Knüpfung der Peptidbindung, Angew. Chem., 97, 79, 1985.
    • (1985) Angew. Chem. , vol.97 , pp. 79
    • Jakubke, H.-D.1    Kuhl, P.2    Könnecke, A.3
  • 481
    • 0021952654 scopus 로고
    • Proteases as catalysts in peptide synthetic chemistry. Shifting the extent of peptide bond synthesis from a "quantité négligeable” to a “quantité considérable”
    • Kullmann, W., Proteases as catalysts in peptide synthetic chemistry. Shifting the extent of peptide bond synthesis from a “quantité négligeable” to a “quantité considérable”, J. Prot. Chem., 4. 1, 1985.
    • (1985) J. Prot. Chem. , vol.4 , pp. 1
    • Kullmann, W.1
  • 482
    • 0006880052 scopus 로고    scopus 로고
    • The use of proteolytic enzymes for the synthesis of specific peptide bonds in globular proteins
    • Offord. R. E. and DiBello, C., Eds., Academic Press, New York
    • Laskowski, M., Jr., The use of proteolytic enzymes for the synthesis of specific peptide bonds in globular proteins, in Semisxnthetic Peptides and Protein, Offord. R. E. and DiBello, C., Eds., Academic Press, New York, 1978, 255.
    • (1978) Semisxnthetic Peptides and Protein , pp. 255
    • Laskowski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.