PROTEOLYTIC SPECIFICITY of 2 HEMORRHAGIC FACTORS, LHF-I and LHF-II, ISOLATED FROM the VENOM of the BUSHMASTER SNAKE (LACHESIS-MUTA-MUTA)

PROTEOLYTIC SPECIFICITY of 2 HEMORRHAGIC FACTORS, LHF-I and LHF-II, ISOLATED FROM the VENOM of the BUSHMASTER SNAKE (LACHESIS-MUTA-MUTA)

Autor Sanchez, E. F. Google Scholar
Cordeiro, M. N. Google Scholar
Deoliveira, E. B. Google Scholar
Juliano, L. Google Scholar
Prado, E. S. Google Scholar
Diniz, C. R. Google Scholar
Instituição FDN EZEQUIEL DIAS
FAC MED RIBEIRAO PRETO
Universidade Federal de São Paulo (UNIFESP)
Resumo Two hemorrhagic metalloproteinases (LHF-I and LHF-II) were previously isolated from Lachesis muta muta (bushmaster snake) venom. the proteolytic activities of these hemorrhagic factors and of the crude venom were investigated using as substrate the oxidized B-chain of bovine insulin. LHF-II cleaves the Ala(14)-Leu(15) bond of insulin B-chain very rapidly and the Phe(24)-Phe(25), His(10)-Leu(11) and His(5)-Leu(6) more slowly, whereas LHF-I hydrolyzed only the Ala(14)-Leu(15) bond. Both hemorrhagic factors cleaved the Leu-Leu bond in the fluorogenic peptide Abz-Pro-Leu-Gly-Leu-Leu-Gly-Arg-EDDnp. When the insulin B-chain was incubated with crude venom previously treated with 2.5 mM PMSF, the Ala(14)-Leu(15) bond was also rapidly cleaved. in addition, the hemorrhagic activity and the digestion of casein remained unaltered. Both hemorrhagic and proteolytic activities were inhibited when the crude venom was treated with EDTA, confirming that only metalloproteinases are responsible for these activities. the hydrolysis of insulin B-chain and the fluorogenic heptapeptide by these proteinases was found to be in inverse relationship to their hemorrhagic activities.
Idioma Inglês
Data de publicação 1995-08-01
Publicado em Toxicon. Oxford: Pergamon-Elsevier B.V., v. 33, n. 8, p. 1061-1069, 1995.
ISSN 0041-0101 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 1061-1069
Fonte http://dx.doi.org/10.1016/0041-0101(95)00040-S
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1995RP65900005
Endereço permanente http://repositorio.unifesp.br/handle/11600/25520

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