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Analysis of phospholipase A2, l ‐amino acid oxidase, and proteinase enzymatic activities of the Lachesis muta rhombeata venom
Author(s) -
Campos Lucas Benício,
Pucca Manuela Berto,
Roncolato Eduardo Crosara,
Netto Joaquim Coutinho,
Barbosa José Elpidio
Publication year - 2012
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21422
Subject(s) - venom , zymography , serine , snake venom , biochemistry , phospholipase a2 , enzyme , phospholipase a , phospholipase , biology , chemistry , microbiology and biotechnology
The study of venom components is an important step toward understanding the mechanism of action of such venoms and is indispensable for the development of new therapies. This work aimed to investigate the venom of Lachesis muta rhombeata and evaluate enzymes related to its toxicity. Phospholipase A2 (PLA 2 ), l ‐amino acid oxidase (LAAO), and proteinase activities were measured, and the molecular weights were estimated. We found the venom to contain one PLA 2 (17 kDa), one LAAO (132 kDa), and three serine proteinases (40, 31, and 20 kDa). Although only serine proteinases were observed in the zymogram, metalloproteinases were found to contribute more to the total proteolytic activity than did serine proteinases. The work confirmed the presence of highly active enzymes; and, moreover, we proposed a novel method for confirming the presence of LAAOs by zymography. We also suggested a simple step to increase the sensitivity of proteinase assays. © 2012 Wiley Periodicals, Inc. J Biochem Mol Toxicol 26:308–314, 2012; View this article online at wileyonlinelibrary.com. DOI 10:1002/jbt.21422