Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/193698
Type: Artigo de periódico
Title: Identification Of A New Vascular Smooth Muscle Contracting Polypeptide In Phoneutria Nigriventer Spider Venom.
Author: Bento, A C
Novello, J C
Marangoni, S
Antunes, E
Giglio, J R
Oliveira, B
de Nucci, G
Abstract: The fractionation of Phoneutria nigriventer spider venom by gel filtration (Sephadex G-10-120) followed by ion-exchange chromatography (microgranular CM-cellulose-52) resulted in sixteen fractions (CI to CXVI) from which CVII+VIII, CIX and CX+XI caused dose-dependent and short-lived contractions of both arterial and venous rabbit vessels. Fraction CX+XI was further purified by a reverse phase HPLC, and a contractile polypeptide (PNV2) was isolated. The amino terminal sequence of PNV2 (LAKRADICQPGKTSQRACET) indicated that it represents a pure polypeptide consisting of a single chain. Furthermore, the amino acid analysis of PNV2 revealed the presence of four disulfide bridges, a high content in Lys (14%), Glx (11%), and the absence of His. The global amino acid composition showed that this polypeptide is composed of 102 residues (Trp not included) with a calculated molecular weight of 12,114. Whether this peptide is responsible for the vascular alterations observed in Phoneutria envenomation, such as lung edema and priapism, remains to be further investigated.
Subject: Amino Acid Sequence
Animals
Male
Molecular Sequence Data
Muscle Contraction
Muscle, Smooth, Vascular
Neuropeptides
Peptides
Rabbits
Spider Venoms
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/8216354
Date Issue: 1993
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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