Biotechnologia Acta Т. 16, No. 2 , 2023
P. 11-12, Bibliography 6, Engl.
UDC: 577.2
DOI: https://doi.org/10.15407/biotech16.02.011

 Full text: (PDF, in English)

FIBRINOGEN-SPECIFIC PROTEASE IN THE Vipera renardi SNAKE VENOM
K.V. BAIDAKOVA^{1, 2}, Y.M. STOHNII², O.M. PLATONOV^2
1Educational and Scientific Center “Institute of Biology and Medicine” of Taras Shevchenko National University of Kyiv, Ukraine
²Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, Kyiv

Aim. To search fibrinogenolytic enzymes among protein components of Vipera renardi snake venom.

Methods. Venom of V. renardi as the lyophilized powder was supplied by Trypillia serpentarium. It was dissolved in 0.05 M Tris-HCl buffer pH 8.3 and fractionated on Superdex G-75 using FPLC system Acta Prime. Peaks were tested for their ability to directly cleave fibrinogen. Hydrolytic products were analyzed by SDS-PAGE. Enzyme-electrophoresis with fibrinogen co-polymerized in 12% polyacrylamide gel was used for the identification of protein that can cleave fibrinogen..

Results. Venom of V. renardi was fractionated on 4 fractions using size-exclusion chromatography. SDS-PAGE of fibrinogen hydrolysis products showed the presence of fibrinogen-specific protease in the 1st and 2nd fractions of venom. 2nd fraction was much more active and according to the data of enzyme electrophoresis contained protease with molecular mass 25 kDa.

Conclusions. Fractionation of V. renardi snake venom allowed to detect a protease with apparent molecular mass 25 kDa that can cleave fibrinogen molecule.
Key-words: proteases, fibrinogen, snake venom, vipera.

© Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, 2022