메뉴 건너뛰기




Volumn 120, Issue 3, 1998, Pages 549-557

Purification and characterization of ovine pancreatic elastase

Author keywords

Affinity chromatography; Elastase; Ovine; Pancreas; Purification

Indexed keywords

PANCREATIC ELASTASE;

EID: 0031811766     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(98)10044-5     Document Type: Article
Times cited : (7)

References (22)
  • 1
    • 0000883637 scopus 로고
    • The elastolytic activity of pancreatic extracts
    • Balo J, Banga J. The elastolytic activity of pancreatic extracts. Biochem J 1950;46:384-7.
    • (1950) Biochem J , vol.46 , pp. 384-387
    • Balo, J.1    Banga, J.2
  • 2
    • 0016363174 scopus 로고
    • The synthesis and analytical use of a highly sensitive and convenient substrate of elastase
    • Bieth J, Spiess B, Wermuth CG. The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biochem Med 1974;11:350-7.
    • (1974) Biochem Med , vol.11 , pp. 350-357
    • Bieth, J.1    Spiess, B.2    Wermuth, C.G.3
  • 3
    • 0024497268 scopus 로고
    • Investigation of the active center of rat pancreatic elastase
    • Bieth JG, Dirrig S, Jung M-L, et al. Investigation of the active center of rat pancreatic elastase. Biochem Biophys Acta 1989;994:64-74.
    • (1989) Biochem Biophys Acta , vol.994 , pp. 64-74
    • Bieth, J.G.1    Dirrig, S.2    Jung, M.-L.3
  • 5
    • 0021773216 scopus 로고
    • Vacuoles are not the sole compartments of proteolytic enzymes in yeast
    • Emter O, Wolf DH. Vacuoles are not the sole compartments of proteolytic enzymes in yeast. FEBS Lett 1984;166:321-5.
    • (1984) FEBS Lett , vol.166 , pp. 321-325
    • Emter, O.1    Wolf, D.H.2
  • 6
    • 0015930533 scopus 로고
    • N-acetyl-(L-Ala)3-p-nitroanilide as a new chromogenic substrate for elastase
    • Feinstein G, Kupfer A, Sokolovsky M. N-acetyl-(L-Ala)3-p-nitroanilide as a new chromogenic substrate for elastase. Biochem Biophys Res Commun 1973;50:1020-6.
    • (1973) Biochem Biophys Res Commun , vol.50 , pp. 1020-1026
    • Feinstein, G.1    Kupfer, A.2    Sokolovsky, M.3
  • 9
    • 0014709196 scopus 로고
    • Isolation and characterization of porcine proelastase
    • Gertler A, Birk Y. Isolation and characterization of porcine proelastase. Eur J Biochem 1970;12:170-6.
    • (1970) Eur J Biochem , vol.12 , pp. 170-176
    • Gertler, A.1    Birk, Y.2
  • 10
    • 0014747224 scopus 로고
    • Acetyl-L-alanyl-L-alanyl-L-alanyl methyl ester: A new higly specific elastase substrate
    • Gertler A, Hofmann T. Acetyl-L-alanyl-L-alanyl-L-alanyl methyl ester: a new higly specific elastase substrate. Can J Biochem 1970;48:384-6.
    • (1970) Can J Biochem , vol.48 , pp. 384-386
    • Gertler, A.1    Hofmann, T.2
  • 11
    • 0017641735 scopus 로고
    • Purification and characterization of porcine elastase II and investigation of its elastolytical specificity
    • Gertler A, Weiss Y, Burstein Y. Purification and characterization of porcine elastase II and investigation of its elastolytical specificity. Biochemistry 1977;16:2709-16.
    • (1977) Biochemistry , vol.16 , pp. 2709-2716
    • Gertler, A.1    Weiss, Y.2    Burstein, Y.3
  • 12
    • 0023046649 scopus 로고
    • Affinity purification of kallikrein and elastase from hog pancreas powder
    • Honda T, Fujita A, Tsubakihara Y, Morihara K. Affinity purification of kallikrein and elastase from hog pancreas powder. J Chromatogr 1986;376:385-93.
    • (1986) J Chromatogr , vol.376 , pp. 385-393
    • Honda, T.1    Fujita, A.2    Tsubakihara, Y.3    Morihara, K.4
  • 13
    • 0026908466 scopus 로고
    • The enzymatic and release characteristics of sheep neutrophil elastase: A comparison with human neutrophil elastase
    • Junger WG, Hallström S, Liu FC, Redl H, Schag G. The enzymatic and release characteristics of sheep neutrophil elastase: a comparison with human neutrophil elastase. Biol Chem Hoppe Seyler 1992;373:691-8.
    • (1992) Biol Chem Hoppe Seyler , vol.373 , pp. 691-698
    • Junger, W.G.1    Hallström, S.2    Liu, F.C.3    Redl, H.4    Schag, G.5
  • 14
    • 0017160779 scopus 로고
    • p-Nitroanilides of 3-carboxypropionyl peptides. Their cleavage by elastase, trypsin and chymotrypsin
    • Kasafirek E, Fric P, Slaby J, Malis F. p-Nitroanilides of 3-carboxypropionyl peptides. Their cleavage by elastase, trypsin and chymotrypsin. Eur J Biochem 1976;69:1-13.
    • (1976) Eur J Biochem , vol.69 , pp. 1-13
    • Kasafirek, E.1    Fric, P.2    Slaby, J.3    Malis, F.4
  • 15
    • 0018115638 scopus 로고
    • One step purification procedure of elastase from pancreatic powder by affinity chromatography
    • Katagiri K, Takeuchi T, Taniguchi K, Sasaki M. One step purification procedure of elastase from pancreatic powder by affinity chromatography. Anal Biochem 1978;86:159-65.
    • (1978) Anal Biochem , vol.86 , pp. 159-165
    • Katagiri, K.1    Takeuchi, T.2    Taniguchi, K.3    Sasaki, M.4
  • 16
    • 0017174488 scopus 로고
    • Purification and characterization of two human pancreatic elastases
    • Largman C, Brodrick JW, Geokas MC. Purification and characterization of two human pancreatic elastases. Biochemistry 1976;15:2491-500.
    • (1976) Biochemistry , vol.15 , pp. 2491-2500
    • Largman, C.1    Brodrick, J.W.2    Geokas, M.C.3
  • 17
    • 0020546301 scopus 로고
    • Isolation and characterization of rat pancreatic elastase
    • Largman C. Isolation and characterization of rat pancreatic elastase. Biochemistry 1983;22:3763-70.
    • (1983) Biochemistry , vol.22 , pp. 3763-3770
    • Largman, C.1
  • 18
    • 0010586561 scopus 로고
    • Pancreatic elastase: Purification, properties, and function
    • Lewis UJ, Williams DE, Brink NG. Pancreatic elastase: purification, properties, and function. J Biol Chem 1956;222:705-20.
    • (1956) J Biol Chem , vol.222 , pp. 705-720
    • Lewis, U.J.1    Williams, D.E.2    Brink, N.G.3
  • 19
    • 0026543741 scopus 로고
    • Identification of elastase in human eosinophils: Immunolocalization, isolation and partial characterization
    • Lungarella G, Menegazzi R, Gardi C, et al. Identification of elastase in human eosinophils: Immunolocalization, isolation and partial characterization. Arch Biochem Biophys 1992;292:128-35.
    • (1992) Arch Biochem Biophys , vol.292 , pp. 128-135
    • Lungarella, G.1    Menegazzi, R.2    Gardi, C.3
  • 20
    • 77956999337 scopus 로고
    • Colowick SP, Kaplan NO, editors. New York: Academic Press
    • Shotton DM. In: Colowick SP, Kaplan NO, editors. Elastase, Methods in Enzymology , vol XIX. New York: Academic Press, 1970:113-140.
    • (1970) Elastase, Methods in Enzymology , vol.19 , pp. 113-140
    • Shotton, D.M.1
  • 21
    • 0016391111 scopus 로고
    • Preparation of adsorbents for biospecific affinity chromatography I. Attachment of group-containing ligands to insoluble polymers by means of bifunctional oxiranes
    • Sundberg L, Porath J. Preparation of adsorbents for biospecific affinity chromatography I. Attachment of group-containing ligands to insoluble polymers by means of bifunctional oxiranes. J Chromatogr 1974;90:87-98.
    • (1974) J Chromatogr , vol.90 , pp. 87-98
    • Sundberg, L.1    Porath, J.2
  • 22
    • 0018627098 scopus 로고
    • Quantitation of proteins solubilized in sodium dodecyl sulfate-mercaptoethanol-Tris electrophoresis buffer
    • Zaman Z, Verwilghen RL. Quantitation of proteins solubilized in sodium dodecyl sulfate-mercaptoethanol-Tris electrophoresis buffer. Anal. Biochem 1979;100:64-9.
    • (1979) Anal. Biochem , vol.100 , pp. 64-69
    • Zaman, Z.1    Verwilghen, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.