HYDROLYTIC SPECIFICITY of 3 BASIC PROTEINASES ISOLATED FROM the VENOM of BOTHROPS-MOOJENI for the B-CHAIN of OXIDIZED INSULIN

HYDROLYTIC SPECIFICITY of 3 BASIC PROTEINASES ISOLATED FROM the VENOM of BOTHROPS-MOOJENI for the B-CHAIN of OXIDIZED INSULIN

Autor Reichl, A. P. Google Scholar
Serrano, SMT Google Scholar
Sampaio, CAM Google Scholar
Mandelbaum, F. R. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo The hydrolytic activity of three basic proteinases isolated from Bothrops moojeni venom was determined on the B-chain of oxidized insulin. the serine proteinases MSP1 and MSP2 cleave the insulin B-chain at identical positions and in the same order of bond cleavage. Cleavage occurs first at the Arg-Gly(22-23) position, followed by hydrolysis of the Lys-Ala(29-30) peptide bond. the metalloproteinase MPB differs from the serine proteinases in cleaving the insulin B-chain very rapidly at four positions: Ser-His(9-10), Ala-Leu(14-15), Tyr-Leu(16-17) and Phe-Phe(24-25).
Idioma Inglês
Data 1993-11-01
Publicado em Toxicon. Oxford: Pergamon-Elsevier B.V., v. 31, n. 11, p. 1479-1482, 1993.
ISSN 0041-0101 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 1479-1482
Fonte http://dx.doi.org/10.1016/0041-0101(93)90213-3
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1993MM43000012
URI http://repositorio.unifesp.br/handle/11600/25359

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