Artículos de revistas
Purification and amino acid sequence of MP-III 4R D49 phospholipase A(2) from Bothrops pirajai snake venom, a toxin with moderate PLA(2) and anticoagulant activities and high myotoxic activity
Registro en:
Journal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 18, n. 3, n. 371, n. 378, 1999.
0277-8033
WOS:000080782300013
10.1023/A:1021051831740
Autor
Toyama, MH
Costa, PD
Novello, JC
de Oliveira, B
Giglio, JR
da Cruz-Hofling, MA
Marangoni, S
Institución
Resumen
MP-III 4R PLA(2) 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 PLA(2) from Bothrops pirajai was determined by amino acid sequencing of reduced and carboxymethylated MP-m 4R and the isolated peptides from clostripain and protease V8 digestion. MP-m 4R is a D49 PLA(2) with 121 amino acid residues and has a molecular weight estimated at 13,800 Da, with 14 half-cysteines. This protein showed moderate PLA(2) and anticoagulant activity. This PLA(2) does not have a high degree of homology with other bothropic PLA(2)-like myotoxins (similar to 75%) and nonbothropic myotoxins (similar to 60%). MP-III 4R is a new PLA(2), 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. 18 3 371 378