Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194174
Type: Artigo de periódico
Title: The Amino Acid Sequence Of Bothropstoxin-ii, An Asp-49 Myotoxin From Bothrops Jararacussu (jararacucu) Venom With Low Phospholipase A2 Activity.
Author: Pereira, M F
Novello, J C
Cintra, A C
Giglio, J R
Landucci, E T
Oliveira, B
Marangoni, S
Abstract: The complete amino acid sequence of bothropstoxin-II (BthTX-II), a myotoxin isolated from Bothrops jararacussu snake venom, is reported. The results show that BthTX-II is an Asp-49 phospholipase A2 (PLA2)-like protein composed of a single polypeptide chain of 120 amino acid residues (Mr = 13,976), containing one methionine and 14 half-cystines. Despite a high degree of homology with other PLA2's and the presence of the strategic residues known to compose the Ca2+-binding loop, namely Tyr-28, Gly-30, Gly-32, and especially Asp-49, besides His-48, Tyr-52, and Asp-99, all of them directly or indirectly involved in catalysis, BthTX-II revealed a very low PLA2 activity when assayed on egg yolk phosphatidylcholine. We attribute this low catalytic activity to the existence of extra mutations, e.g., Trp-5 for Phe-5, which points to the need of considering other strategic positions, since only Lys-49 PLA2's have been considered to be devoid of this enzymatic activity.
Subject: Amino Acid Sequence
Animals
Aspartic Acid
Bothrops
Chromatography, High Pressure Liquid
Crotalid Venoms
Electrophoresis, Polyacrylamide Gel
Group Ii Phospholipases A2
Hydrolysis
Molecular Sequence Data
Phospholipases A
Phospholipases A2
Reptilian Proteins
Serine Endopeptidases
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/9619591
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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