메뉴 건너뛰기




Volumn , Issue , 2001, Pages 103-122

An orientation to edman chemistry

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84963500747     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (53)
  • 1
    • 0000369624 scopus 로고
    • A method for the determination of the amino acid sequence in peptides
    • Edman, P., A method for the determination of the amino acid sequence in peptides, Arch. Biochem., 22, 475–476, 1949.
    • (1949) Arch. Biochem. , vol.22 , pp. 475-476
    • Edman, P.1
  • 2
    • 0009052101 scopus 로고
    • Degradation of peptides by the Edman method with direct identification of the PTH-amino acid
    • Schroeder, W., Degradation of peptides by the Edman method with direct identification of the PTH-amino acid, Meth. Enzymol., 11, 445–475, 1967.
    • (1967) Meth. Enzymol. , vol.11 , pp. 445-475
    • Schroeder, W.1
  • 4
    • 85056928221 scopus 로고
    • Analysis of amino acid phenylthiohydantoins by gas chromatography and high-performance liquid chromatography, in Protein Sequence Determination, Needleman, S. B., Ed. Springer-Verlag, New York, also listed as
    • Pisano, J. J., Analysis of amino acid phenylthiohydantoins by gas chromatography and high-performance liquid chromatography, in Protein Sequence Determination, Needleman, S. B., Ed. Springer-Verlag, New York, also listed as Mol. Biol. Biochem. Biophys., 8, 280–296, 1975.
    • (1975) Mol. Biol. Biochem. Biophys. , vol.8 , pp. 280-296
    • Pisano, J.J.1
  • 5
    • 0006273338 scopus 로고
    • Subtractive Edman degradation
    • Konigsberg, W., Subtractive Edman degradation, Meth. Enzymol., 25, 326–332, 1972.
    • (1972) Meth. Enzymol. , vol.25 , pp. 326-332
    • Konigsberg, W.1
  • 6
    • 0342982221 scopus 로고
    • Sequence analysis with dansyl chloride
    • Gray, W. R., Sequence analysis with dansyl chloride, Meth. Enzymol., 25, 332–344, 1972.
    • (1972) Meth. Enzymol. , vol.25 , pp. 332-344
    • Gray, W.R.1
  • 7
    • 0017690243 scopus 로고
    • Improved manual sequencing methods
    • Tarr, G. E., Improved manual sequencing methods, Meth. Enzymol., 47, 335–357, 1977.
    • (1977) Meth. Enzymol. , vol.47 , pp. 335-357
    • Tarr, G.E.1
  • 8
    • 77957009275 scopus 로고
    • A., Automatic solid-phase Edman degradation
    • Laursen, R. A., Automatic solid-phase Edman degradation, Meth. Enzymol., 25, 344–359, 1972.
    • (1972) Meth. Enzymol. , vol.25 , pp. 344-359
    • Laursen, R.1
  • 9
    • 0017813965 scopus 로고
    • Polyquaternary amines prevent peptide loss from sequenators
    • Tarr, G., Beecher, J. F., Bell, H., and McKean, D. J., Polyquaternary amines prevent peptide loss from sequenators, Anal. Biochem., 84, 622–627, 1978.
    • (1978) Anal. Biochem. , vol.84 , pp. 622-627
    • Tarr, G.1    Beecher, J.F.2    Bell, H.3    McKean, D.J.4
  • 10
    • 0017346884 scopus 로고
    • Rapid analysis of amino acid phenylthiohydantoins by high performance liquid chromatography
    • Zimmerman, C. L., Appella, E., and Pisano, J. J., Rapid analysis of amino acid phenylthiohydantoins by high performance liquid chromatography, Anal. Biochem., 77, 569–573, 1977.
    • (1977) Anal. Biochem. , vol.77 , pp. 569-573
    • Zimmerman, C.L.1    Appella, E.2    Pisano, J.J.3
  • 11
    • 0020677397 scopus 로고
    • Manual micro-sequence analysis of polypeptides using dimethylami-noazobenzene isothiocyanate
    • Chang, J. Y., Manual micro-sequence analysis of polypeptides using dimethylami-noazobenzene isothiocyanate, Meth. Enzymol., 91, 455–466, 1983.
    • (1983) Meth. Enzymol. , vol.91 , pp. 455-466
    • Chang, J.Y.1
  • 12
    • 0017721414 scopus 로고
    • Identification of anilinothiazolinones after rapid conversion to N-α-phenylthiocarbamylamino acid methylamides
    • Inman, J. K. and Appella, E., Identification of anilinothiazolinones after rapid conversion to N-α-phenylthiocarbamylamino acid methylamides, Meth. Enzymol., 47, 374–384, 1977.
    • (1977) Meth. Enzymol. , vol.47 , pp. 374-384
    • Inman, J.K.1    Appella, E.2
  • 14
    • 0020667308 scopus 로고
    • Radiochemical sequence analysis of biosynthetically labeled proteins
    • Coligan, J. E., Gates, F. T., III, Kimball, E. S., and Maloy, W. L., Radiochemical sequence analysis of biosynthetically labeled proteins, Meth. Enzymol., 91, 413–434, 1983.
    • (1983) Meth. Enzymol. , vol.91 , pp. 413-434
    • Coligan, J.E.1    Gates, F.T.2    Kimball, E.S.3    Maloy, W.L.4
  • 15
    • 0017168413 scopus 로고
    • A device coupled to a modified sequenator for the automated conversion of anilinothiazolinones into PTH amino acids
    • Wittman-Liebold, B., Graffunder, H., and Kohls, H., A device coupled to a modified sequenator for the automated conversion of anilinothiazolinones into PTH amino acids, Anal. Biochem., 75, 621–633, 1976.
    • (1976) Anal. Biochem. , vol.75 , pp. 621-633
    • Wittman-Liebold, B.1    Graffunder, H.2    Kohls, H.3
  • 16
  • 25
    • 0000114026 scopus 로고
    • Use of cyanate for determining amino-terminal residues in proteins
    • Stark, G. R., Use of cyanate for determining amino-terminal residues in proteins, Meth. Enzymol., 11, 125–138, 1967.
    • (1967) Meth. Enzymol. , vol.11 , pp. 125-138
    • Stark, G.R.1
  • 26
    • 0027518907 scopus 로고
    • N-isopropyliodoacetamide in the reduction and alkylation of proteins: Use in microsequence analysis
    • Krutzsch, H. C. and Inman, J. K., N-isopropyliodoacetamide in the reduction and alkylation of proteins: use in microsequence analysis, Anal. Biochem., 209, 109–116, 1993.
    • (1993) Anal. Biochem. , vol.209 , pp. 109-116
    • Krutzsch, H.C.1    Inman, J.K.2
  • 27
    • 85056958180 scopus 로고
    • Of Urfs and Orfs, University Science Books, Mill Valley, CA
    • Doolittle, R., Of Urfs and Orfs, University Science Books, Mill Valley, CA, 1987.
    • (1987)
    • Doolittle, R.1
  • 28
    • 0023547917 scopus 로고
    • Identification of disulfide-bridged substructures within human von Willebrand factor
    • Marti, T., Rösselet, S. J., Titani, K., and Walsh, K., Identification of disulfide-bridged substructures within human von Willebrand factor, Biochemistry, 26, 8099–8109, 1987.
    • (1987) Biochemistry , vol.26 , pp. 8099-8109
    • Marti, T.1    Rösselet, S.J.2    Titani, K.3    Walsh, K.4
  • 31
    • 85056984433 scopus 로고    scopus 로고
    • Unpublished
    • Hempel, J., Unpublished.
    • Hempel, J.1
  • 32
    • 0023895386 scopus 로고
    • Identification of hormone-interacting amino acid residues within the steroid-binding domain of the glucocorticoid receptor in relation to other steroid hormone receptors
    • Carlstedt-Duke, J, Strömstedt, P.-E., Persson, B., Cederlund, E., Gustafsson, J.-Å., and Jörnvall, H., Identification of hormone-interacting amino acid residues within the steroid-binding domain of the glucocorticoid receptor in relation to other steroid hormone receptors, J. Biol. Chem., 263, 6842–6848, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6842-6848
    • Carlstedt-Duke, J.1    Strömstedt, P.-E.2    Persson, B.3    Cederlund, E.4    Gustafsson, J.-Å.5    Jörnvall, H.6
  • 33
    • 0021763486 scopus 로고
    • Aldehyde dehydrogenase from human liver: Primary structure of the cytoplasmic isoenzyme
    • Hempel, J., von Bahr-Lindström, H., and Jörnvall, H., Aldehyde dehydrogenase from human liver: primary structure of the cytoplasmic isoenzyme, Eur. J. Biochem., 141, 21–35, 1984.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 21-35
    • Hempel, J.1    von Bahr-Lindström, H.2    Jörnvall, H.3
  • 34
    • 0025021579 scopus 로고
    • Isolation and structural characterization of three forms of recombinant consensus α-interferon
    • Klein, M. L., Bartley, T. D., Davis, J. M., Whiteley, D. W., and Lu, H. S., Isolation and structural characterization of three forms of recombinant consensus α-interferon, Arch. Biochem. Biophys., 276, 531–537, 1990.
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 531-537
    • Klein, M.L.1    Bartley, T.D.2    Davis, J.M.3    Whiteley, D.W.4    Lu, H.S.5
  • 36
    • 0022508657 scopus 로고
    • Sequence determinants of cytosolic N-terminal protein processing
    • Flinta, C., Persson, B., Jörnvall, H., and von Heijne, G., Sequence determinants of cytosolic N-terminal protein processing, Eur. J. Biochem., 154, 193–196, 1986.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 193-196
    • Flinta, C.1    Persson, B.2    Jörnvall, H.3    von Heijne, G.4
  • 37
    • 0030641446 scopus 로고    scopus 로고
    • On-membrane deblocking of proteins, in Protein Sequencing Protocols, Smith, B. J., Ed., Humana Press, Totowa
    • Hirano, H., Komatsu, S., and Tsunasawa, S., On-membrane deblocking of proteins, in Protein Sequencing Protocols, Smith, B. J., Ed., Humana Press, Totowa, NJ, 1997, chap. 27, 285–292.
    • NJ, 1997, Chap , vol.27 , pp. 285-292
    • Hirano, H.1    Komatsu, S.2    Tsunasawa, S.3
  • 38
    • 85056962796 scopus 로고    scopus 로고
    • Deacetylation and internal cleavage of polypeptides for N-terminal sequence analysis
    • Atassi, M. Z. and Appella, E., Eds., Plenum Press, New York, 1994
    • Gheorge, M. T. and Bergman, T., Deacetylation and internal cleavage of polypeptides for N-terminal sequence analysis, in Methods in Protein Structure Analysis, Atassi, M. Z. and Appella, E., Eds., Plenum Press, New York, 1994.
    • Methods in Protein Structure Analysis
    • Gheorge, M.T.1    Bergman, T.2
  • 39
    • 85056922340 scopus 로고    scopus 로고
    • 39
    • Based on the cumulative compositions of 195, 891 proteins in the PIR databank (67.9 million residues) at this writing.
  • 40
    • 80053113166 scopus 로고
    • Cleavage at aspartyl-prolyl bonds
    • Landon, M., Cleavage at aspartyl-prolyl bonds, Meth. Enzymol., 47, 145–149, 1977.
    • (1977) Meth. Enzymol. , vol.47 , pp. 145-149
    • Landon, M.1
  • 41
    • 0017637022 scopus 로고
    • Cleavage at Asn-Gly bonds with hydroxylamine
    • Bornstein, P. and Balian, G., Cleavage at Asn-Gly bonds with hydroxylamine, Meth. Enzymol., 47, 132–145, 1977.
    • (1977) Meth. Enzymol. , vol.47 , pp. 132-145
    • Bornstein, P.1    Balian, G.2
  • 43
    • 0028983813 scopus 로고
    • Improvement of an “In-gel” digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Góñez, J., and Heldin, C.-I., Improvement of an “In-gel” digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing, Anal. Biochem., 224, 451–455, 1994.
    • (1994) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Góñez, J.3    Heldin, C.-I.4
  • 44
    • 85056975144 scopus 로고    scopus 로고
    • Commentary posted on the Association of Biological Resource Facilities (ABRF) electronic bulletin board, archives available at http://www.abrf.org.
  • 45
    • 0019880508 scopus 로고
    • Use of fluorescamine as an effective blocking reagent to reduce the background in protein sequence analyses by the Beckman automated sequenator
    • Bhown, A. S., Bennett, J. C., Morgan, P. H., and Mole, J. E., Use of fluorescamine as an effective blocking reagent to reduce the background in protein sequence analyses by the Beckman automated sequenator, Anal. Biochem., 112, 158–162, 1981.
    • (1981) Anal. Biochem. , vol.112 , pp. 158-162
    • Bhown, A.S.1    Bennett, J.C.2    Morgan, P.H.3    Mole, J.E.4
  • 46
    • 0021115839 scopus 로고    scopus 로고
    • Sequence analysis of rat hypothalamic corticotropin-releasing factor with the o-phthalaldehyde strategy
    • Spiess, J., Rivier, J., and Vale, W., Sequence analysis of rat hypothalamic corticotropin-releasing factor with the o-phthalaldehyde strategy, Biochemistry, 22, 4341–4346, 1988.
    • Biochemistry , vol.22 , pp. 4341-4346
    • Spiess, J.1    Rivier, J.2    Vale, W.3
  • 47
    • 0017854338 scopus 로고
    • Neisseria pili proteins: Amino-terminal amino acid sequences and identification of an unusual amino acid
    • Hermodson, M. A., Chen, K. C. S., and Buchanan, T. M., Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid, Biochemistry, 17, 442–445, 1978.
    • (1978) Biochemistry , vol.17 , pp. 442-445
    • Hermodson, M.A.1    Chen, K.C.S.2    Buchanan, T.M.3
  • 48
    • 0017858156 scopus 로고
    • A novel Edman-type degradation: Direct formation of the thiohydantoin ring in alkaline solution by reaction of Edman-type reagents with N-monomethyl amino acids
    • Chang, J.-Y., A novel Edman-type degradation: direct formation of the thiohydantoin ring in alkaline solution by reaction of Edman-type reagents with N-monomethyl amino acids, FEBS Lett., 91, 63–68, 1978.
    • (1978) FEBS Lett , vol.91 , pp. 63-68
    • Chang, J.-Y.1
  • 49
    • 0023043042 scopus 로고
    • Internal chain cleavage and product heterogeneity during Edman degradation of isosteric peptide analogs lacking the α-carbonyl function
    • Hempel, J., Nilsson, K., Larsson, K., and Jörnvall, H., Internal chain cleavage and product heterogeneity during Edman degradation of isosteric peptide analogs lacking the α-carbonyl function, FEBS Lett., 194, 333–337, 1986.
    • (1986) FEBS Lett , vol.194 , pp. 333-337
    • Hempel, J.1    Nilsson, K.2    Larsson, K.3    Jörnvall, H.4
  • 50
    • 0025935237 scopus 로고
    • J., Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • Duclos, B., Marcandier, S., and Cozzone, A. J., Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis, Meth. Enzymol., 201, 10–21, 1991.
    • (1991) Meth. Enzymol. , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A.3
  • 52
    • 0026015290 scopus 로고
    • Determination and location of phosphoserine in proteins and peptides by conversion to S-ethylcysteine
    • Meyer, H. E., Hoffmann-Posorske, E., and Heilmeyer, L. M. G., Determination and location of phosphoserine in proteins and peptides by conversion to S-ethylcysteine, Meth. Enzymol., 201, 169–185, 1991.
    • (1991) Meth. Enzymol. , vol.201 , pp. 169-185
    • Meyer, H.E.1    Hoffmann-Posorske, E.2    Heilmeyer, L.M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.