ISSN 1995-5537
"Biotechnology" journal Vol. 3, No. 1, 2010
Р. 27-34, Bibliography 29, Ukranian.
Universal Decimal classification: 577.151.6
National Taras Shevchenko University, Kyiv
Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, Kyiv
Proteinase that demonstrated fibrinogenase activity from the venom of Echis multisquamatis was purified. Molecular weight of enzyme determined by SDS PAGE was 35 ± 1 kDа. Inhibitory assay showed that fibrinogenase belonged to the serine type of proteinases. It hydrolyzed X-X-R- pNa derivatives of tripeptides and splitted Bβ-chain of fibrinogen. Molecular weight of removed peptide of Bβ-chain allowed to suppose that fibrinogenase splitted ВβR23-E24 peptide bound. The Km value of this reaction was 8 µM.
Key words: β- fibrinogenase, fibrinogen, venom of Echis multisquamatis.
© Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, 2008