Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58462
Type: Artigo de periódico
Title: Purification and initial characterization of a novel protein with factor Xa activity from Lonomia obliqua caterpillar spicules
Author: Lilla, S
Pereira, R
Hyslop, S
Donato, JL
Le Bonniec, BF
de Nucci, G
Abstract: A novel protein with factor Xa-like activity was isolated from Lonomia obliqua caterpillar spicules by gel filtration chromatography and reversed-phase high-performance liquid chromatography. The protein had a mass of 20745.7 Da, as determined by mass spectrometry, and contained four Cys residues. Enzymatic hydrolysis followed by de novo sequencing by tandem mass spectrometry was used to determine the primary structure of the protein and the cysteine residues linked by disulfide bridges. The positions of 24 sequenced tryptic peptides, including the N-terminal, were deduced by comparison with a homologous protein from the superfamily Bombycoidea. Approximately 90% of the primary structure of the active protein was determined. Copyright (c) 2005 John Wiley A Sons, Ltd.
Subject: blood coagulation
caterpillars
factor Xa
envenoming
electrospray time-of-flight mass spectrometry
Country: Inglaterra
Editor: John Wiley & Sons Ltd
Rights: fechado
Identifier DOI: 10.1002/jms.802
Date Issue: 2005
Appears in Collections:Unicamp - Artigos e Outros Documentos

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