Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194674
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 C
Novello,
Marangoni, S
Abstract: The PLA2 and crotapotin subunits of crotoxin from Crotalus durissus cascavella venom were purified by a combination of high-performance liquid chromatography (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 degrees C. 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.
Subject: Amino Acids
Animals
Chromatography, Gel
Chromatography, High Pressure Liquid
Crotalid Venoms
Crotalus
Crotoxin
Electrophoresis, Polyacrylamide Gel
Enzyme Inhibitors
Phospholipases A
Phospholipases A2
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/11307952
Date Issue: 2000
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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