Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/193743
Type: Artigo de periódico
Title: Biochemical Characterization Of A Vascular Smooth Muscle Contracting Polypeptide Purified From Phoneutria Nigriventer (armed Spider) Venom.
Author: Marangoni, S
Borges, N C
Marangoni, R A
Antunes, E
Vieira, C A
Novello, J C
Domont, G B
Giglio, J R
Oliveira, B
de Nucci, G
Abstract: Biochemical characterization of a vascular smooth muscle contracting polypeptide purified from Phoneutria nigriventer (armed spider) venom. Toxicon 31, 377-384, 1993. Crude Phoneutria nigriventer venom was fractionated by Sephadex, ion-exchange and reverse-phase high performance liquid chromatography. One protein (PNV1) with spasmogenic activity in rabbit vascular smooth muscle was isolated and biochemically characterized. PNV1 has 125 amino acid residues and a calculated mol. wt of 13,899. Special features of the amino acid composition of PNV1 are the presence of two disulfide bridges and the high percentage (27%) of Asx and Glx. The N-terminal amino acid sequence indicates that PNV1 is different from other polypeptides isolated from Phoneutria nigriventer venom.
Subject: Amino Acid Sequence
Animals
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
In Vitro Techniques
Indicators And Reagents
Male
Molecular Sequence Data
Muscle Contraction
Muscle, Smooth, Vascular
Peptides
Rabbits
Spider Venoms
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/8503129
Date Issue: 1993
Appears in Collections:Unicamp - Artigos e Outros Documentos

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