Purification and Characterization of a Metalloproteinase with Weak Fibrinogenolytic Activity from Naja atra Venom
- VernacularTitle:眼镜蛇毒中一个弱纤维蛋白原水解活性金属蛋白酶的纯化和性质研究
- Author:
Qianyun SUN
;
Min LI
;
Fumei YANG
- Publication Type:Journal Article
- Keywords:
metallopmteinase;
fibrinogenase;
snake venom;
Naja atra
- From:
Chinese Journal of Biochemistry and Molecular Biology
2007;23(10):835-843
- CountryChina
- Language:Chinese
-
Abstract:
A novel fibrinogenolytic protease,named atrase A,has been purified from the venom of Naja atra by sequential chromatography.Atrase A is a single chain glycoprotein with a molecular weight of 64.6 kD,an isoelectric point of pH 9.6 and a neutral sugar content of 4.16%.Atrase A specifically and slowly degraded α-chain of fibrinogen.This fibrinogenolytic activity Was inhibited by chelating agents(EDTA,EGTA and 1,10-phenanthroline)and DTY,and partially inhibited by PMSF,but not by soybean trypsin inhibitor,indicating it is a metalloproteinase.Atrase A showed edema-inducing activity and bactericidal activity against Staphylococcusa aureus.Atrase A did not show cytotoxicity on A549 and K562 cells in MTT assay,but detached adherent A549 cells from the substrate.Atrase A did not show significant inhibition of platelet aggregation induced by ADP or collagen,and did not exhibit proteolytic activities towards fibrin,azocasein and BAEE.It also did not show hemorrhage activity when injected subcutaneously into mice.
