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Volumn 3, Issue 2, 1997, Pages 93-98

Enzymatic peptide synthesis in frozen aqueous solution: Use of Nα-unprotected peptide esters as acyl donors

Author keywords

Enzymatic peptide synthesis; Frozen system; N unprotected substrates; chymotrypsin

Indexed keywords

CHYMOTRYPSIN; DIPEPTIDE; ESTER; OLIGOPEPTIDE; WATER;

EID: 0031090827     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-1387(199703)3:2<93::aid-psc87>3.0.co;2-r     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 0025258501 scopus 로고
    • Enzyme catalysed peptide synthesis in ice
    • M. Schuster, A. Aaviksaar and H.-D. Jakubke (1990). Enzyme catalysed peptide synthesis in ice. Tetrahedron 46, 8093-8102.
    • (1990) Tetrahedron , vol.46 , pp. 8093-8102
    • Schuster, M.1    Aaviksaar, A.2    Jakubke, H.-D.3
  • 2
    • 3043002579 scopus 로고
    • Thermodynamically controlled α-chymotrypsin-catalysed peptide synthesis in frozen aqueous solutions
    • DWI - Reports. Nos 112A/B, D. Brandenburg, V. T. Ivanov and W. Voelter, Eds., Verlag Mainz, Aachen 1993
    • M. Schuster, H.-D. Jakubke and A. Aaviksaar (1993). Thermodynamically controlled α-chymotrypsin-catalysed peptide synthesis in frozen aqueous solutions in: Chemistry of Peptides and Proteins, Vols 5/6, DWI - Reports. Nos 112A/B, D. Brandenburg, V. T. Ivanov and W. Voelter, Eds., p. 203-209, Verlag Mainz, Aachen 1993.
    • (1993) Chemistry of Peptides and Proteins , vol.5-6 , pp. 203-209
    • Schuster, M.1    Jakubke, H.-D.2    Aaviksaar, A.3
  • 3
    • 0026342581 scopus 로고
    • Protease-catalysed peptide synthesis in frozen aqueous systems: The 'freeze-concentratlon model'
    • M. Schuster, A. Aaviksaar, M. Haga, U. Ullmann and H.-D. Jakubke (1991). Protease-catalysed peptide synthesis in frozen aqueous systems: The 'freeze-concentratlon model'. Biomed. Biochim Acta. 50, 84-89.
    • (1991) Biomed. Biochim Acta. , vol.50 , pp. 84-89
    • Schuster, M.1    Aaviksaar, A.2    Haga, M.3    Ullmann, U.4    Jakubke, H.-D.5
  • 4
    • 0012079141 scopus 로고
    • C. H. Schneider and A. Eberle, Eds., ESCOM, Leiden
    • G. Ullmann and H.-D. Jakubke in: Peptides 1992, C. H. Schneider and A. Eberle, Eds., p. 36-37, ESCOM, Leiden 1993.
    • (1993) Peptides 1992 , pp. 36-37
    • Ullmann, G.1    Jakubke, H.-D.2
  • 5
    • 0027283814 scopus 로고
    • Chymotrypsin-catalysed peptide synthesis in ice: Use of unprotected amino acids as acyl donors
    • M. Schuster, G. Ullmann, U. Ullmann and H.-D. Jakubke (1993). Chymotrypsin-catalysed peptide synthesis in ice: Use of unprotected amino acids as acyl donors. Tetrahedron Lett. 34, 5701-5702.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 5701-5702
    • Schuster, M.1    Ullmann, G.2    Ullmann, U.3    Jakubke, H.-D.4
  • 6
    • 0027326646 scopus 로고
    • Peptide synthesis by chymotrypsin in frozen solutions. Free amino acids as nucleophiles
    • V. Tougo, H. Meos, M. Haga, A. Aaviksaar and H.-D. Jakubke (1993). Peptide synthesis by chymotrypsin in frozen solutions. Free amino acids as nucleophiles. FEBS Lett 329, 40-42.
    • (1993) FEBS Lett , vol.329 , pp. 40-42
    • Tougo, V.1    Meos, H.2    Haga, M.3    Aaviksaar, A.4    Jakubke, H.-D.5
  • 9
    • 0028675931 scopus 로고
    • Enzymatic peptide synthesis in frozen aqueous systems: Influence of modified reaction conditions on the peptide yield
    • S. Gerisch, G. Ullmann, K. Stubenrauch and H.-D. Jakubke (1994). Enzymatic peptide synthesis in frozen aqueous systems: Influence of modified reaction conditions on the peptide yield. Biol. Chem. Hoppe-Seyler. 375, 825-828.
    • (1994) Biol. Chem. Hoppe-Seyler. , vol.375 , pp. 825-828
    • Gerisch, S.1    Ullmann, G.2    Stubenrauch, K.3    Jakubke, H.-D.4
  • 10
    • 0028950788 scopus 로고
    • Die Verwendung von Ficin zur Knüpfung der Peptidbindungen in gefrorenen wässrigen Sytemen
    • M. Hänsler, H. Keilhack and H.-D. Jakubke (1995). Die Verwendung von Ficin zur Knüpfung der Peptidbindungen in gefrorenen wässrigen Sytemen. Pharmazie 50, 184-187.
    • (1995) Pharmazie , vol.50 , pp. 184-187
    • Hänsler, M.1    Keilhack, H.2    Jakubke, H.-D.3
  • 11
    • 0029361858 scopus 로고
    • The application of papain, ficin and clostripain in kinetically controlled peptide synthesis in frozen aqueous solutions
    • M. Hänsler, G. Ullmann and H.-D. Jakubke (1995). The application of papain, ficin and clostripain in kinetically controlled peptide synthesis in frozen aqueous solutions. J. Peptide Science, 1, 283-287.
    • (1995) J. Peptide Science , vol.1 , pp. 283-287
    • Hänsler, M.1    Ullmann, G.2    Jakubke, H.-D.3
  • 12
    • 0001026076 scopus 로고
    • Kinetics of reactions in frozen solution
    • R. E. Pincock and T. E. Kiovsky (1966). Kinetics of reactions in frozen solution. J. Chem. Ed. 43, 358-360.
    • (1966) J. Chem. Ed. , vol.43 , pp. 358-360
    • Pincock, R.E.1    Kiovsky, T.E.2
  • 13
    • 0002118940 scopus 로고
    • R. B. Duckworth, Ed., Academic Press Inc., London
    • O. Fennema in: Water Relations of Food, R. B. Duckworth, Ed., p.539-556. Academic Press Inc., London 1975.
    • (1975) Water Relations of Food , pp. 539-556
    • Fennema, O.1
  • 16
    • 0000965118 scopus 로고
    • Enzymatic synthesis of short peptides in heterogeneous mixtures of substrates
    • I. Gill and E. N. Vulfson (1993). Enzymatic synthesis of short peptides in heterogeneous mixtures of substrates. J. Am. Chem. Soc. 115, 3348-3349.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3348-3349
    • Gill, I.1    Vulfson, E.N.2
  • 18
  • 19
    • 0014211618 scopus 로고
    • On the size of the active site of proteases. I. Papain
    • I. Schechter and A. Berger (1967). On the size of the active site of proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 20
    • 0020092264 scopus 로고
    • Kinetic investigation of the α-chymotrypsin-catalysed hydrolysis of peptide substrates. The relationship between the peptide structure C-terminal to the cleave bond and reactivity
    • S. A. Bizzozero, W. K. Baumann and H. Dutler (1982). Kinetic investigation of the α-chymotrypsin-catalysed hydrolysis of peptide substrates. The relationship between the peptide structure C-terminal to the cleave bond and reactivity. Eur. J. Biochem. 122, 251-258.
    • (1982) Eur. J. Biochem. , vol.122 , pp. 251-258
    • Bizzozero, S.A.1    Baumann, W.K.2    Dutler, H.3
  • 21
    • 0022648161 scopus 로고
    • A spectrophotometric assay for the characterization of the S' subsite specificity of α-chymotrypsin
    • V. Schellenberger and H.-D. Jakubke (1986). A spectrophotometric assay for the characterization of the S' subsite specificity of α-chymotrypsin. Biochim. Biophys. Acta 869, 54-60.
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 54-60
    • Schellenberger, V.1    Jakubke, H.-D.2
  • 22
    • 0344521572 scopus 로고
    • Salt-enhanced aminoalysis of acyl-α-chymotrypsins by dipeptides
    • V. Schellenberger, A. Aaviksaar and H.-D. Jakubke (1990). Salt-enhanced aminoalysis of acyl-α-chymotrypsins by dipeptides. Biocatalysis 4, 291-296.
    • (1990) Biocatalysis , vol.4 , pp. 291-296
    • Schellenberger, V.1    Aaviksaar, A.2    Jakubke, H.-D.3
  • 23
    • 0025064289 scopus 로고
    • Characterization of the S' subsite specificity of bovine pancreatic α-chymotrypsin via acyl transfer
    • V. Schellenberger, U. Schellenberger, Y. V. Mitin and H.-D. Jakubke (1990). Characterization of the S' subsite specificity of bovine pancreatic α-chymotrypsin via acyl transfer. Eur. J. Biochem 187, 163-167.
    • (1990) Eur. J. Biochem , vol.187 , pp. 163-167
    • Schellenberger, V.1    Schellenberger, U.2    Mitin, Y.V.3    Jakubke, H.-D.4
  • 24
    • 0025892385 scopus 로고
    • Electrostatic effects in the α-chymotrypsin-catalysed acyl transfer. I. Influence of different inorganic salts
    • V. Schellenberger, M. Kosk, H.-D. Jakubke and A. Aaviksaar (1991). Electrostatic effects in the α-chymotrypsin-catalysed acyl transfer. I. Influence of different inorganic salts. Biochim. Biophys. Acta 1078, 1-7.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 1-7
    • Schellenberger, V.1    Kosk, M.2    Jakubke, H.-D.3    Aaviksaar, A.4
  • 25
    • 0025892386 scopus 로고
    • Electrostatic effects in the α-chymotrypsin-catalysed acyl transfer. II. Efficiency of nucleophiles bearing charged groups in various locations
    • V. Schellenberger, H.-D. Jakubke and V. Kasche (1991). Electrostatic effects in the α-chymotrypsin-catalysed acyl transfer. II. Efficiency of nucleophiles bearing charged groups in various locations. Biochim. Biophys. Acta 1078, 8-11.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 8-11
    • Schellenberger, V.1    Jakubke, H.-D.2    Kasche, V.3
  • 26
    • 0015518520 scopus 로고
    • Structure of crystalline α-chymotrypsin. V. The atomic structure of tosyl-α-chymotiypsin at 2Å resolution
    • J. J. Birktoft and D. M. Blow (1972). Structure of crystalline α-chymotrypsin. V. The atomic structure of tosyl-α-chymotiypsin at 2Å resolution. J. Mol. Biol. 68, 187-240.
    • (1972) J. Mol. Biol. , vol.68 , pp. 187-240
    • Birktoft, J.J.1    Blow, D.M.2
  • 27
    • 0025737760 scopus 로고
    • The specificity of chymotrypsin. A statistical analysis of hydrolysis data
    • V. Schellenberger, K. Braune, H.-J. Hofmann and H.-D. Jakubke (1991). The specificity of chymotrypsin. A statistical analysis of hydrolysis data. Eur. J. Biochem. 199, 623-636.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 623-636
    • Schellenberger, V.1    Braune, K.2    Hofmann, H.-J.3    Jakubke, H.-D.4
  • 28
    • 0015926434 scopus 로고
    • Kinetic investigations of the α-chymotrypsin-catalysed hydrolysis of peptide substrates. The relationship between the peptide-structure N-terminal to the cleave bond and reactivity
    • W. K. Baumann, S. A. Bizzozero and H. Dutler (1973). Kinetic investigations of the α-chymotrypsin-catalysed hydrolysis of peptide substrates. The relationship between the peptide-structure N-terminal to the cleave bond and reactivity. Eur. J. Biochem. 39, 381-391.
    • (1973) Eur. J. Biochem. , vol.39 , pp. 381-391
    • Baumann, W.K.1    Bizzozero, S.A.2    Dutler, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.