Purification and characterization of a phospholipase A2 isoenzyme isolated from Lachesis muta snake venom.
Biochem Pharmacol
; 63(9): 1589-97, 2002 May 01.
Article
em En
| MEDLINE
| ID: mdl-12007562
ABSTRACT
A new phospholipase A2 (PLA2) isoenzyme was isolated from Lachesis muta crude venom, and was named LM-PLA2-II. This enzyme was purified by gel filtration on a Sephacryl S-200 HR column followed by reverse-phase chromatography on a C2/C18 column. LM-PLA2-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 PLA2s from several sources. LM-PLA2-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-PLA2-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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfolipases A
/
Venenos de Víboras
/
Viperidae
/
Isoenzimas
Limite:
Animals
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article