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Type: Artigo de periódico
Title: Cytotoxic Action In Myoblasts And Myotubes (c2c12) And Enzymatic Characterization Of A New Phospholipase A2 Isoform (bj-v) From Bothrops Jararacussu Venom
Author: Bonfim V.L.
Ponce-Soto L.A.
Novello J.C.
Marangoni S.
Abstract: A new PLA2 Bj-V from Bothrops jararacussu (14039.49 Da determined by MALDI-TOF mass spectrometry) was isolated in only one chromatographic step by HPLC ion-exchange and its purity was confirmed by reverse phase. Amino acid analysis showed a high content of hydrophobic and basic amino acids as well as 14 half-cysteine residues. The N-terminal sequence (DLWQFGQMIL KETGKIPFPY YGAYGCYCGW GGRGGKPKDG TDRCCYVHD . . .) showed a high degree of homology with basic D49 PLA2 myotoxins from other Bothrops venoms. Bj V showed discrete sigmoidal enzymatic behavior, with maximal activity at pH 8.4 and 35-40°C. Full PLA2 activity required Ca 2+ (10 mM) and there was little catalytic activity in the presence of 1 mM Ca2+.The addition of Mn2+ or Mg2+ (10 mM) in the presence of low (1 mM) Ca2+ slightly increased the enzyme activity, whereas Zn2+ and Cu2+ (10 mM) diminished the activity. The substitution of Ca2+ for Mg2+ or Cu 2+ also reduced the enzymatic activity. Bj V had PLA2 activity and produced cytotoxicity in murine C2C12 skeletal muscle myoblasts and myotubes. The isolation of these isoforms Bj-IV [1] and Bj-V (described herein) found in a fraction previously described as homogeneous shows us the importance of optimization in purification techniques in order to better understand their biological behavior. © 2006 Bentham Science Publishers Ltd.
Rights: fechado
Identifier DOI: 10.2174/092986606777790520
Date Issue: 2006
Appears in Collections:Unicamp - Artigos e Outros Documentos

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