BASIC PROTEINASES FROM BOTHROPS-MOOJENI-(CAISSACA) VENOM .2. ISOLATION of the METALLOPROTEINASE MPB - COMPARISON of the PROTEOLYTIC ACTIVITY ON NATURAL SUBSTRATES BY MPB, MSP-1 and MSP-2

BASIC PROTEINASES FROM BOTHROPS-MOOJENI-(CAISSACA) VENOM .2. ISOLATION of the METALLOPROTEINASE MPB - COMPARISON of the PROTEOLYTIC ACTIVITY ON NATURAL SUBSTRATES BY MPB, MSP-1 and MSP-2

Autor Serrano, SMT Google Scholar
Sampaio, CAM Google Scholar
Mandelbaum, F. R. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo A basic metalloproteinase active on casein was isolated from Bothrops moojeni venom by chromatography on Sephadex G-100, DEAE-Sephacel, SP-Sephadex C-50 and Sepharose 12. the enzyme, named MPB, is not hemorrhagic and presents only traces of blood-clotting activity. On polyacrylamide gel electrophoresis at pH 4.3, MPB presented a single and diffuse protein band. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the enzyme presented two protein bands corresponding to mol. wts of 65,000 and 55,000, which stained with Schiff's reagent. the proteolytic activity of MPB was inhibited by ethylenediaminetetracetate, 1,10-phenanthroline and dithiothreitol. the proteolytic activity of MPB and the serine proteinases MSP 1 and MSP 2 on natural substrates indicates differences in hydrolytic specificity among these enzymes. All fibrinogen chains were degraded by the three proteinases, but MPB is the most active. On fibrin, the proteinases hydrolyzed only the alpha-chain and alpha-polymer, leaving the beta-chain and gamma-dimer apparently untouched. the native type I collagen was partially hydrolyzed by the three enzymes but no digestion product was detected. On the contrary, calf and guinea-pig skin type I gelatins were readily digested by MSP 1 and MSP 2 producing different hydrolysis patterns. MPB was the least active proteinase on the gelatins. the digestion of fibronectin showed an inversion in the specificity of these proteinases. MPB was the most active on fibronectin, while MSP 1 and MSP 2 promoted a faint, partial hydrolysis on this protein.
Idioma Inglês
Data de publicação 1993-04-01
Publicado em Toxicon. Oxford: Pergamon-Elsevier B.V., v. 31, n. 4, p. 483-492, 1993.
ISSN 0041-0101 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 483-492
Fonte http://dx.doi.org/10.1016/0041-0101(93)90183-J
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1993KY87900012
Endereço permanente http://repositorio.unifesp.br/handle/11600/25317

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