Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/107295
Type: Artigo de periódico
Title: Enzymatic Characterization Of A Novel Phospholipase A2 From Crotalus Durissus Cascavella Rattlesnake (maracambóia) Venom
Author: Beghini D.G.
Toyama M.H.
Hyslop S.
Sodek L.
Novelle 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 reversephase 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 35-40oC. 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. © 2000 Plenum Publishing Corporation.
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Rights: fechado
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Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-52849118877&partnerID=40&md5=dcec1c1e373eec12ecb4401e3826dc89
Date Issue: 2000
Appears in Collections:Unicamp - Artigos e Outros Documentos

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