ISSN:
1573-4943
Keywords:
Bothrops pirajai
;
D49 PLA2
;
anticoagulant PLA2
;
amino acid sequence
;
PrTX-III
;
MP-III 4R
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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 (~75%) and nonbothropic myotoxins (~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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1021051831740
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