Prothrombin-Sepharose-Purified Factor V and Its Role in Prothrombin Conversion | Zendy

Twee-Hee Ong | Zendy

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Prothrombin-Sepharose-Purified Factor V and Its Role in Prothrombin Conversion

Author(s) -

Twee-Hee Ong

Publication year - 2017

Publication title -

asean journal on science and technology for development

Language(s) - English

Resource type - Journals

eISSN - 2224-9028

pISSN - 0217-5460

DOI - 10.29037/ajstd.221

Subject(s) - sepharose , prothrombin complex , chemistry , chromatography , thrombin , affinity chromatography , prothrombin complex concentrate , biochemistry , coagulation , biology , medicine , immunology , enzyme , warfarin , platelet , atrial fibrillation

Bovine Factor V isolated by the method of Esnouf and Jobin (1967) has been further purified by affiniy chromotgraphy through prothrombin-sepharose. Factor V bound quantitative to the prothrombin-sepharose column. There was a 2-fold increase in the average specific activity (260.000 units/mg protein) of the Factor V recovered. Recovery of total Factor V activity and total protein was about 95% and 90% respectively.

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