Purification and characterization of a phospholipase A2 isoenzyme isolated from Lachesis muta snake venom

被引：68
作者：
Fully, AL
de Miranda, ALP
Zingali, RB
Guimaraes, JA
机构：
[1] Univ Fed Rio Grande do Sul, Ctr Biotecnol, BR-91501970 Porto Alegre, RS, Brazil
[2] Univ Fed Rio de Janeiro, Inst Ciencias Biomed, Dept Bioquim Med, BR-21945 Rio De Janeiro, RJ, Brazil
[3] Univ Fed Rio de Janeiro, Fac Farm, BR-21945 Rio De Janeiro, RJ, Brazil
来源：
BIOCHEMICAL PHARMACOLOGY | 2002年 / 63卷 / 09期
关键词：
Lachesis muta venom; purification of phospholipase A(2); platelet aggregation; edema; myotoxicity; lysophosphatidylcholine;
D O I：
10.1016/S0006-2952(02)00873-0
中图分类号：
R9 [药学];
学科分类号：
1007 ;
摘要：
A new phospholipase A(2) (PLA(2)) isoenzyme was isolated from Lachesis muta crude venom, and was named LM-PLA(2)-II. This enzyme was purified by gel filtration on a Sephacryl S-200 HR column followed by reverse-phase chromatography on a C-2/C-18 column. LM-PLA(2)-II consists of a single polypeptide chain with an apparent molecular mass of 18 kDa and an isoelectric point at pH 5.4. The amino terminal sequence of the enzyme revealed a high degree of homology with other PLA(2)s from several sources. LM-PLA(2)-II has a high indirect hemolytic activity and a potent inhibitory effect on platelet aggregation induced by ADP and collagen. It also produces a significant paw edema reaction in rats. The edematous response in rats was abolished by pretreatment with either indomethacin or dexamethasone, suggesting the involvement of cyclo-oxygenase. Pretreatment of LM-PLA(2)-II with p-bromophenacyl bromide abolished all of these actions, clearly indicating that the biological activities, including the edematogenic effect, are dependent entirely on its enzymatic activity. (C) 2002 Elsevier Science Inc. All rights reserved.
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收藏
页码：1589 / 1597
页数：9
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