A New Phospholipase A2 from Lachesis muta rhombeata: Purification, Biochemical and Comparative Characterization with Crotoxin B

被引：10
|
作者：
Cordeiro, Francielle A. [1 ]
Perini, Tiberio G. K. [1 ]
Bregge-Silva, Cristiane [1 ]
Cremonez, Caroline M. [1 ]
Rodrigues, Renata S. [2 ]
Boldrini-Franca, Johara [1 ]
Bordon, Karla de C. F. [1 ]
De Souza, Dayane L. N. [2 ]
Ache, David C. [2 ]
Rodrigues, Veridiana de M. [2 ]
dos Santos, Wagner F. [3 ]
Rosa, Jose C. [4 ,5 ]
Arantes, Eliane C. [1 ]
机构：
[1] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Fis & Quim, Sao Paulo, Brazil
[2] Univ Fed Uberlandia, Inst Genet & Bioquim, BR-38400 Uberlandia, MG, Brazil
[3] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, Sao Paulo, Brazil
[4] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogen, Sao Paulo, Brazil
[5] Ctr Quim Prot, Sao Paulo, Brazil
来源：
PROTEIN AND PEPTIDE LETTERS | 2015年 / 22卷 / 09期
基金：
巴西圣保罗研究基金会;
关键词：
Acidic phospholipase A(2); crotoxin B; edema; Lachesis muta rhombeata; myotoxicity; snake venom; CROTALUS-DURISSUS-TERRIFICUS; SNAKE-VENOM; FUNCTIONAL-CHARACTERIZATION; LMTX-I; ISOFORMS; VIPERIDAE; MYOTOXINS; MECHANISM; PROTEINS; ENZYMES;
D O I：
10.2174/0929866522666150706112431
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Phospholipases A(2) (PLA(2)s) are enzymes responsible for inflammatory effects, edema formation, myotoxicity, neurotoxicity and other manifestations from envenoming. In this paper we report the isolation and biochemical characterization of Lmr-PLA(2), the first acidic PLA(2) found in Lachesis muta rhombeata venom. Furthermore, this study compared biological effects of Lmr-PLA(2) and crotoxin B (CB), a PLA(2) from Crotalus durissus terrificus venom. Lmr-PLA(2) was isolated by molecular exclusion and reversed phase chromatography. The purified enzyme showed a molecular mass of 13,975 Da, pI of 5.46 and its partial amino acid sequence showed a high identity with PLA(2)s already described in the literature. In addition, this enzyme possesses the residue D49 in its amino acid sequence, indicating that it is a catalytically active PLA(2). Lmr-PLA(2) presented high phospholipase activity and was able to inhibit platelet aggregation. Studies of biochemical characterization of new PLA(2)s, as Lmr-PLA(2), are relevant since they help to clarify the structure-function relationship of this important class of toxins.
引用
收藏
页码：816 / 827
页数：12
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