Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/107074
Type: Artigo de periódico
Title: Enzymatic Characterization Of A Novel Phospholipase A2 From Crotalus Durissus Cascavella Rattlesnake (maracambòia) Venom
Author: Beghini D.G.
Toyama M.H.
Hyslop S.
Sodek L.
Novello J.C.
Marangoni S.
Abstract: The PLA2 and crotapotin subunits of crotoxin from Crotalus durissus cascavella venom were purified by a combination of HPLC molecular exclusion (Protein Pack 300SW column) and reverse-phase HPLC (RP-HPLC). Tricine SDS-PAGE showed that the PLA2 and crotapotins migrated as single bands with estimated molecular masses of 15 and 9 kDa, respectively. The amino acid composition of the PLA2 showed the presence of 14 half-cysteines and a high content of basic residues (Lys, Arg, His), whereas the crotapotins were rich in hydrophobic, negatively charged residues and half-cysteines. The PLA2 showed allosteric behavior, with maximal activity at pH 8.3 and 35-40°C. The C. d. cascavella PLA2 required Ca2+ for activity, but was inhibited by Cu2+ and Zn2+ and by Cu2+ and Mg2+ in the presence and absence of Ca2+, respectively. Crotapotin (F3) and heparin inhibited the catalytic activity of the PLA2 by acting as allosteric inhibitors.
Editor: 
Rights: fechado
Identifier DOI: 10.1023/A:1007123329817
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0034468565&partnerID=40&md5=426fe547540c2743fca6556ba82e7e5c
Date Issue: 2000
Appears in Collections:Unicamp - Artigos e Outros Documentos

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