Purification and characterization of platelet aggregation inhibitor component from venom of agkistrodon halys pallas.
- Author:
Ping LIU
1
;
Jian-Min XU
;
Qian JIN
;
Yi-Qing WANG
;
Hong ZHU
;
Yuan-Cong ZHOU
Author Information
1. Department of Hematology, Zhongshan Hospital, Fudan University, Shanghai, 200032 China.
- Publication Type:Journal Article
- MeSH:
Crotalid Venoms;
analysis;
Humans;
Oligopeptides;
chemistry;
Platelet Aggregation;
drug effects;
Platelet Aggregation Inhibitors;
isolation & purification
- From:
Journal of Experimental Hematology
2004;12(2):194-198
- CountryChina
- Language:Chinese
-
Abstract:
Snake venom proteins,particularly from the viper and elapid families, have been known to contain a number of platelet active components including what cause platelet aggregation or inhibit platelet aggregation. Some of them have potential clinical usefulness for the treatment of human hemorrhagic or thrombotic disease. Agkistrodon halys pallas belonging to viper family is only growing in China. The aim of this study was to purify a human platelet aggregation inhibitor from venom of Agkistrodon halys pallas and determine its biochemical character. Whether a component could inhibit human platelet aggregation was act as a method to follow the tracks of the protein. Crude venom of Agkistrodon halys pallas was loaded onto a DEAE-Sepharose CL-6B chromatography column could gain 6 peaks. A platelet inhibitor with molecular mass of 65 kD on SDS-PAGE, was purified from peak 2 by Sephadex G-75 gel filtration and SP-Sepharose, Mono Q on FPLC. It could inhibit human platelet aggregation induced by ADP, collagen without activities of phospholipase A2, esterase, fibrinogenolytic. It is concluded that a platelet inhibitor can be isolated and purified from venom of Agkistrodon halys pallas and its inhibition of platelet aggregation is does-dependent.
