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Titolo:
Inhibition of mutalysin II, a metalloproteinase from bushmaster snake venom by human alpha 2-macroglobulin and rabbit immunoglobulin
Autore:
Souza, CT; Moura, MB; Magalhaes, A; Heneine, LGD; Olortegui, CC; Diniz, CR; Sanchez, EF;
Indirizzi:
Fdn Ezequiel Dias, Ctr Pesquisa & Desanvolvimento, BR-30510010 Belo Horizonte, MG, Brazil Fdn Ezequiel Dias Belo Horizonte MG Brazil BR-30510010 BConte, MG, Brazil
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 2, volume: 130, anno: 2001,
pagine: 155 - 168
SICI:
1096-4959(200109)130:2<155:IOMIAM>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
LACHESIS-MUTA-MUTA; MACROGLOBULIN RAT ALPHA-1-INHIBITOR-3; CLEAVAGE SITES; HEMORRHAGIC METALLOPROTEINASES; HUMAN ALPHA-2-MACROGLOBULIN; PROTEINASE BINDING; BAIT REGION; LHF-II; PURIFICATION; MECHANISM;
Keywords:
mutalysins; alpha-macroglobulins; snake venom; lachesis muta; metalloproteinases; reprolysin; antibodies; enzyme inhibition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Sanchez, EF Fdn Ezequiel Dias, Ctr Pesquisa & Desanvolvimento, BR-30510010Belo Horizonte, MG, Brazil Fdn Ezequiel Dias Belo Horizonte MG Brazil BR-30510010 BCazil
Citazione:
C.T. Souza et al., "Inhibition of mutalysin II, a metalloproteinase from bushmaster snake venom by human alpha 2-macroglobulin and rabbit immunoglobulin", COMP BIOC B, 130(2), 2001, pp. 155-168

Abstract

Mutalysin II is a 22.5-kDa zinc endopeptidase isolated from Lachesis muta muta snake venom. In order to determine whether the inhibitors human alpha2-macroglobulin (alpha2-M) and rabbit antibody to mutalysin II share a common mechanism, we have investigated the inhibition of mutalysin II by these two different glycoproteins. The proteolytic activity of mutalysin II with dimethylcasein as substrate was completely inhibited by human alpha2-M and by a purified rabbit antibody to mutalysin II. The protection of fibrin(ogen) digestion by alpha2-M was slightly better than the protection offered by the antibody. In addition, the purified antibody reacted only with the metalloproteinase in bushmaster venom, as demonstrated by immunodiffusion. SDS-PAGE analysis of reduced samples showed that the interaction of mutalysin II with alpha2-M resulted in the formation of high molecular complex (similar to 180000) and M-r 90000 fragments generated by the venom enzyme. Also, fragments at 85 and 23 kDa were detected under non-reducing conditions afterincubation of rabbit immunoglobulin with enzyme. Proteolysis of dimethylcasein as substrate revealed that the stoichiometry of inhibition was 1.0 molof human alpha2-M. and 1.5 mol of rabbit IgG antimutalysin II per mole of enzyme. Furthermore, dimethylcasein hydrolysis indicated that several viperid snake venoms, including Bothrops atrox, B. alternatus and Trimeresurus flavoviridis cross-reacted with the specific rabbit antibody to varying degrees. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 21:58:48