Purification and characteristic of the protein c activator from agkistrodon halys halys snake venom

   


1. Palladin Institute of Biochemistry, National Academy of Sciences
Type: Experimental/clinical study
PubMed Id: 16119100
Year: 2003 vol: 49  issue:5  pages: 470-478
Abstract: Protein C activator from Agkistrodon halys halys venom has been purified by ion-exchange and gel-filtration chromatography. The purified enzyme consists of a single peptide chain with molecular weight of 34 kD. Its pH-optimum was the range of 7,5-8,0. The enzyme was inhibited by DFP, benzamidine, PMSF, EGTA. Protein C activator was as effective as Protac (Pentapharm AG, Switzerland) for determination of protein C level in blood plasma using APTT test and protein C chromogenic substrate.
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Reference: Gornitskaya O.V., Platonova T.N., Purification and characteristic of the protein c activator from agkistrodon halys halys snake venom, Biomeditsinskaya khimiya, 2003, vol: 49(5), 470-478.
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