The purification and identification of phospholipid-binding anticoagulation protein from agkistrodon halys brevicaudus venom / 中国药理学通报
Chinese Pharmacological Bulletin
;
(12)2003.
Artículo
en Chino
| WPRIM
| ID: wpr-559461
ABSTRACT
Aim To purify Phospholipid-binding anticoagulation protein(PBAP) from Agkistrodon halys Brevicaudus Venom and study the biochemical characterization.Methods The Phospholipid-binding anticoagulation protein was purified from Agkistrodon halys Brevicaudus Venom by Cation ion exchange chromatography on CM Sephadex C-25 and negative ion exchange chromatography on DEAE Sepharose CL-6B,gel filtration on Sephacryl S-200 and Sephadex G-75 chromatography.Its anticoagulant activities in vitro were assayed by activated partial thromboplastin time(APTT);its molecular weight was calculated by SDS-polyacrylamide gel electrophoresis(SDS-PAGE) and its isoelectric point was estimated by the isoelectric focusing electrophoresis.Binding experiments of anticoagulation protein to phospholipids vesicles were performed with thinlayer chromatography.Results A kind of protein was purified from Agkistrodon halys Brevicaudus Venom which was able to prolong APTT.The SDSPAGE showed that it was dimer and its molecular weight was 24.0?10~3 under non-reducing condition and 14.6?10~3 under reducing condition.The isoelectric point was pH 5.2 by the isoelectric focusing electrophoresis.Having arginine ester-hydrolyzing enzyme and binding Phospholipid activify,its effect on APTT was activity stronger with concentration increasing.Conclusion It is a successful method of the purification of Phospholipid-binding anticoagulation protein from the Agkistrodon halys Brevicaudus Venom.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Tipo de estudio:
Estudio diagnóstico
Idioma:
Chino
Revista:
Chinese Pharmacological Bulletin
Año:
2003
Tipo del documento:
Artículo
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