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Identification and partial purification of an anticoagulant factor from the venom of the Iranian snake Agkistrodon halys 80
Ghorbanpur,M; Zare Mirakabadi,A; Zokaee,F; Zolfagarrian,H.
An anticoagulant factor was purified from the venom of the Iranian snake Agkistrodon halys by gel filtration on Sephadex G-50 and ion-exchange chromatography on DEAE-Sepharose. In the final stage of purification, the percentage recovery of purified anticoagulant factor was found to be 83%. The purified anticoagulant factor revealed a single protein band in SDS-polyacrylamide electrophoresis under reducing conditions and its molecular weight was about 22 kDa. The purified peptide did not show any effect on casein, BApNA or plasma.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; Agkistrodon halys; Anticoagulant factor; Chromatography.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000100010
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Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys 80
Ghorbanpur,M; Zare Mirakabadi,A; Zokaee,F; Zolfagarrian,H; Rabiei,H.
Agkistrodon halys is one of several dangerous snake species in Iran. Among the most important signs and symptoms in patients envenomated by this snake is disseminated intravascular coagulation. A thrombin-like enzyme, called AH143, was isolated from Agkistrodon halys venom by gel filtration on a Sephadex G-50 column, ion-exchange chromatography on a DEAE-Sepharose and high performance liquid chromatography (HPLC) on a C18 column. In the final stage of purification, 0.82 mg of purified enzyme was obtained from 182.5 mg of venom. The purified enzyme showed a single protein band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), under reducing conditions, and its molecular mass was found to be about 30 kDa. AH143 revealed clotting...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Iranian snake; Venom; Agkistrodon halys; Serine protease; Chromatography; Coagulant activity.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992009000300005
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