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Volumn 1, Issue , 2004, Pages 1037-1039

Peptidyl-Asp metalloendopeptidase

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EID: 38749083026     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50334-7     Document Type: Chapter
Times cited : (4)

References (13)
  • 2
    • 0018848604 scopus 로고
    • Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi
    • G.R. Drapeau (1980) Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi. J. Biol. Chem. 255 839-840.
    • (1980) J. Biol. Chem. , vol.255 , pp. 839-840
    • Drapeau, G.R.1
  • 3
    • 0023689153 scopus 로고
    • A new commercially available endoproteinase which cleaves specifically at the amino terminal side of aspartic acid
    • S. Fischer, U. Geuss, M. Schäffer, G.-B. Kresse and G.R. Drapeau (1988) A new commercially available endoproteinase which cleaves specifically at the amino terminal side of aspartic acid. J. Protein Chem. 7 225-226.
    • (1988) J. Protein Chem. , vol.7 , pp. 225-226
    • Fischer, S.1    Geuss, U.2    Schäffer, M.3    Kresse, G.-B.4    Drapeau, G.R.5
  • 4
    • 10244249396 scopus 로고
    • Characterization of glutamyl cleavage activity of endoproteinase Asp-N sequencing grade
    • U. Geuss, M. Schäffer, J. Tschakert and G.-B. Kresse (1990) Characterization of glutamyl cleavage activity of endoproteinase Asp-N sequencing grade. J. Protein Chem. 9 299-300.
    • (1990) J. Protein Chem. , vol.9 , pp. 299-300
    • Geuss, U.1    Schäffer, M.2    Tschakert, J.3    Kresse, G.-B.4
  • 6
    • 0024342419 scopus 로고
    • Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins
    • D. Ingrosso, A.V. Fowler, J. Bleibaum and S. Clarke (1989) Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins. Biochem. Biophys. Res. Commun. 162 1524-1528.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1524-1528
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 7
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type I recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • C.K. Leonard, M.W. Spellman, L. Riddle, R.J. Harris, J.N. Thomas and T.J. Gregory (1990) Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type I recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265 10373-10382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 8
    • 0018606895 scopus 로고
    • Isolation and properties of the protease from the wild-type and mutant stains of Pseudomonas fragi
    • J. Noreau and G.R. Drapeau (1979) Isolation and properties of the protease from the wild-type and mutant stains of Pseudomonas fragi. J. Bacteriol. 140 911-916.
    • (1979) J. Bacteriol. , vol.140 , pp. 911-916
    • Noreau, J.1    Drapeau, G.R.2
  • 9
    • 0011920142 scopus 로고
    • Use of a metalloproteinase specific for the amino side of Asp in protein sequencing
    • B. Wittmann-Liebold (Ed.), Berlin and Heidelberg: Springer
    • H. Ponstingl, G. Maier, M. Little and E. Krauhs (1986) Use of a metalloproteinase specific for the amino side of Asp in protein sequencing. B. Wittmann-Liebold (Ed.) Advanced Methods in Protein Microsequence Analysis Berlin and Heidelberg: Springer 316-319.
    • (1986) Advanced Methods in Protein Microsequence Analysis , pp. 316-319
    • Ponstingl, H.1    Maier, G.2    Little, M.3    Krauhs, E.4
  • 10
    • 0016671111 scopus 로고
    • Isolation of an extracellular neutral protease from Pseudomonas fragi
    • M.A. Porzio and A.M. Pearson (1975) Isolation of an extracellular neutral protease from Pseudomonas fragi. Biochim. Biophys. Acta 384 235-241.
    • (1975) Biochim. Biophys. Acta , vol.384 , pp. 235-241
    • Porzio, M.A.1    Pearson, A.M.2
  • 11
    • 0029051493 scopus 로고
    • Molecular cloning and sequence analysis of flavastacin: an O-glycosylated procaryotic zinc metalloendopeptidase
    • A.L. Tarentino, G. Quinones, B.G. Grimwood, C.R. Hauer and T.H. Plummer Jr. (1995) Molecular cloning and sequence analysis of flavastacin: an O-glycosylated procaryotic zinc metalloendopeptidase. Arch. Biochem. Biophys. 319 281-285.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 281-285
    • Tarentino, A.L.1    Quinones, G.2    Grimwood, B.G.3    Hauer, C.R.4    Plummer, T.H.5
  • 12
    • 0025672602 scopus 로고
    • Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues
    • T. Tetaz, J.R. Morrison, J. Andreou and N.H. Fidge (1990) Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues. Biochem. Int. 22 561-566.
    • (1990) Biochem. Int. , vol.22 , pp. 561-566
    • Tetaz, T.1    Morrison, J.R.2    Andreou, J.3    Fidge, N.H.4
  • 13
    • 84944118150 scopus 로고
    • Charakterisierung der Endoprotease Asp N [Characterization of endoprotease Asp N].
    • University of Munich.
    • Tschakert, J. (1989) Charakterisierung der Endoprotease Asp N [Characterization of endoprotease Asp N]. Diploma thesis, University of Munich.
    • (1989) Diploma thesis,
    • Tschakert, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.