Isolation,characterization and biological activity of a plasminogen activator from Gloydius brevicaudus venom
- VernacularTitle:短尾蝮蛇毒纤溶酶原激活剂的分离纯化及活性测定
- Author:
Zhiqiang ZHANG
;
Jinhua ZHANG
;
Ruiming YU
;
Yuna LI
;
Jianji CHEN
;
Yunlu XU
- Publication Type:Journal Article
- Keywords:
Gloydius brevicaudus venom;
plasminogen activator;
Affinity chromatography;
reversed phase chromatography;
characterization;
biological activity
- From:
Chinese Pharmacological Bulletin
2003;0(12):-
- CountryChina
- Language:Chinese
-
Abstract:
Aim To isolate and purify a novel plasminogen activator(PA)from Gloydius brevicaudus venom(GBV)and study characterization and biological activities of GBV-PA.Methods Affinity chromatography in Benzamidine Sepharose 6B(AC)and Lichrospher C-18 4.6/250 reversed phase chromatography(RPC)were used for isolation and purification;SDS-PAGE was used to detect molecular weight(MW);Disc polyacrylamide gel eletrophoresis was used to measure the point of isoelectric(pI);Chromogenic substrate method was used to observe the biological activities.Results A novel GBV-PA which its purification reached the homogeneity level was isolated and purified from GBV by AC and RPC;The MW of the novel GBV-PA was 3.26?104 and the pI was 5.2;The novel GBV-PA activated human plasminogen specifically and the special activity was 2.87 t-PA IU?mg-1;Moreover,our results indicated that this novel GBV-PA was a serine proteinase which had no affinity to fibrin.Conclusion A novel GBV-PA that can be isolated and purificated from GBV by AC and RPC was proved to be a serine protease and has no affinity to fibrin.
