FURTHER CHARACTERIZATION of BOTHROPAIN, A CYSTEINE PEPTIDASE FROM the PLASMA of the SNAKE BOTHROPS-JARARACA

FURTHER CHARACTERIZATION of BOTHROPAIN, A CYSTEINE PEPTIDASE FROM the PLASMA of the SNAKE BOTHROPS-JARARACA

Autor Carmona, E. Google Scholar
Portaro, FCV Google Scholar
Juliano, L. Google Scholar
Picarelli, Z. P. Google Scholar
Prado, E. S. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
INST BUTANTAN
Resumo 1. A new procedure was developed for the isolation of bothropain from Bothrops jararaca plasma. the previously used proteolytic digestion step was abolished and HPLC was introduced for the final purification.2. Comparison of enzyme preparations obtained by the two procedures demonstrated a weak proteolysis of bothropain by trypsin, which had no effect on its catalytic properties.3. the primary specificity of bothropain for basic amino acids was confirmed and extended to the S-benzyl-cysteinyl residue. the enzyme showed a strong specificity for hydrophobic groups at P2, with a marked preference for Leu over Phe. No hydrolysis of oxidized insulin B chain by bothropain was detected. Binding of peptidyl diazomethane was also favored by hydrophobic residues at P2 but a restricted specificity for P1 was not observed.4. the catalytic properties, and the inhibition pattern by diazomethanes, indicate a similarity between bothropain and cathepsin L.
Idioma Inglês
Data 1993-03-01
Publicado em Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. Oxford: Pergamon-Elsevier B.V., v. 104, n. 3, p. 599-606, 1993.
ISSN 0305-0491 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 599-606
Fonte http://dx.doi.org/10.1016/0305-0491(93)90288-G
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1993KR27900025
URI http://repositorio.unifesp.br/handle/11600/25312

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