Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195335
Type: Artigo de periódico
Title: Structural And Functional Characterization Of Basic Pla2 Isolated From Crotalus Durissus Terrificus Venom.
Author: Oliveira, D G
Toyama, M H
Novello, J C
Beriam, L O S
Marangoni, S
Abstract: The venom of Crotalus durissus terrificus was fractionated by reverse-phase HPLC to obtain crotapotins (F5 and F7) and PLA2 (F15, F16, and F17) of high purity. The phospholipases A2 (PLA2S) and crotapotins showed antimicrobial activity against Xanthomonas axonopodis pv. passiflorae, although the unseparated crotoxin did not. The F17 of the PLA2 also revealed significant anticoagulant activity, althrough for this to occur the presence of Glu 53 and Trp 61 is important. The F17 of the PLA2 showed allosteric behavior in the presence of a synthetic substrate. The amino acid sequence of this PLA2 isoform, determined by automatic sequencing, was HLLQFNKMLKFETRK NAVPFYAFGCYCGWGGQRRPKDATDRCCFVHDCCYEKVTKCNTKWDFYRYSLKSGY ITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPDSRCREPSETC. Analysis showed that the sequence of this PLA2 isoform differed slightly from the amino acid sequence of the basic crotoxin subunit reported in the literature. The homology with other crotalid PLA2 cited in the literature varied from 60% to 90%. The pL was estimated to be 8.15, and the calculated molecular weight was 14664.14 as determined by Tricine SDS-PAGE, two-dimensional electrophoresis, and MALDI-TOFF. These results also suggested that the enzymatic activity plays an important role in the bactericidal effect of the F17 PLA2 as well as that of anticoagulation, although other regions of the molecule may also be involved in this biological activity.
Subject: Amino Acid Sequence
Animals
Anti-bacterial Agents
Anticoagulants
Catalysis
Chromatography, High Pressure Liquid
Crotalid Venoms
Crotalus
Crotoxin
Electrophoresis, Polyacrylamide Gel
Enzyme Inhibitors
Isoenzymes
Kinetics
Molecular Sequence Data
Phospholipases A
Phospholipases A2
Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization
Xanthomonas
Citation: Journal Of Protein Chemistry. v. 21, n. 3, p. 161-8, 2002-Mar.
Rights: fechado
Address: http://www.ncbi.nlm.nih.gov/pubmed/12018617
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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