Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194376
Type: Artigo de periódico
Title: Purification And Amino Acid Sequence Of Mp-iii 4r D49 Phospholipase A2 From Bothrops Pirajai Snake Venom, A Toxin With Moderate Pla2 And Anticoagulant Activities And High Myotoxic Activity.
Author: Toyama, M H
Costa, P D
Novello, J C
de Oliveira, B
Giglio, J R
da Cruz-Höfling, M A
Marangoni, S
Abstract: MP-III 4R PLA2 was purified from the venom of Bothrops pirajai venom (Bahia's jararacussu) after three chromatographic steps which started with RP-HPLC. The complete amino acid sequence of MP-III 4R PLA2 from Bothrops pirajai was determined by amino acid sequencing of reduced and carboxymethylated MP-III 4R and the isolated peptides from clostripain and protease V8 digestion. MP-III 4R is a D49 PLA2 with 121 amino acid residues and has a molecular weight estimated at 13,800 Da, with 14 half-cysteines. This protein showed moderate PLA2 and anticoagulant activity. This PLA2 does not have a high degree of homology with other bothropic PLA2-like myotoxins (approximately 75%) and nonbothropic myotoxins (approximately 60%). MP-III 4R is a new PLA2, which was isolated using exclusively analytical and preparative HPLC methods. Based on the N-terminal sequence and biological activities, MP-III 4R was identified as similar to piratoxin-III (PrTX-III), which was isolated by conventional chromatography based on molecular exclusion ion exchange chromatography. Clinical manifestations indicate that at the site of toxin injection, there may be pain of variable intensity, because animals continue to lick the limb. No clinical sign indicating general toxicity was noticed. Myotoxicity was observed in gastrocnemius muscle cells after exposure to MP-III 4R, with a high frequency (70%) of affected muscle fibers.
Subject: Amino Acid Sequence
Animals
Anticoagulants
Bothrops
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Group Ii Phospholipases A2
Mice
Molecular Sequence Data
Muscle, Skeletal
Peptides
Phospholipases A
Phospholipases A2
Reptilian Proteins
Sequence Analysis
Sequence Homology, Amino Acid
Snake Venoms
Time Factors
Toxins, Biological
Viper Venoms
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/10395455
Date Issue: 1999
Appears in Collections:Unicamp - Artigos e Outros Documentos

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