Structure-Activity Relationship of Phospholipase A2s Isolated from Vipera aspis Venom.
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Date
2012-04
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Abstract
To elucidate the structure-activity relationship of snake venom phospholipase A2,
the primary structures of two phospholipase A2s from V. aspis venom were analyzed, and
the three-dimensional conformation models were compared.
Study Design: Cross-sectional study.
Place and Duration of Study: Department of Microbiology, Faculty of Pharmacy, Meijo
University, between August 2009 and June 2011.
Methodology: The primary structures of purified phospholipase A2-II and -III were
analyzed by Edman sequencing. Three-dimensional models of these enzymes and
previously reported phospholipase A2-I (Vaspin) were constructed by the homology
modeling method.
Results: Both phospholipase A2-II and –III were found to be monomeric proteins which
consist of 121 and 122 amino acid residues, respectively. Their primary structures were
consistent with the deduced sequence obtained from genomic DNA analysis. The
molecular models of both enzymes indicated that the substitution of important amino acid
residues for anticoagulant and lethal activity might have caused the relatively weak
toxicity.
Conclusion: The structure-activity relationship of PLA2s was clarified by using molecular
models, and clear understanding was obtained.
Description
Keywords
Phospholipase A2, snake venom, structure, computer model
Citation
Komori Yumiko, Nakamura Yasuo, Yunokuchi Izumi, Nikai Toshiaki. Structure-Activity Relationship of Phospholipase A2s Isolated from Vipera aspis Venom. International Journal of Biochemistry Research & Review 2012 Apr-Jun ; 2(2) : 50-59.