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Journal archive > 2006 > N 6 November-December


V. L. Karbovskiy1,2, М. Y. Levkiv1, A. N. Savchuk2, O. V. Gornitskaya2, G. L. Volkov2, Ts. Bukhan3

1Taras Shevchenko Kyiv National University, Ukraine;
2Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
3Shidjir International Co., Mongolia, Ulaanbaatar;
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Plasminogen activator “Ahh-32” from Agkistrodon halys halys venom has been isolated and purified using affinity and ion-exchange chromatography. The purified enzyme consists of the single peptide-chain with molecular weigth of 32?kDa. It can convert free plasminogen into active form?– plasmin. “Ahh-32” was inhibited by DFP and benzamidine. Besides, the enzyme influen­ces significantly the activation of plasminogen by streptokinase without having effect on analogical process in case of usage of tissue tipe plasminogen activator. The obtained protein can be used as an instrument under investigation of protein-protein interactions in haemostasis system.

Key words: snake venom, Agkistrodon halys halys, plasminogen activator.

The original article in Ukrainian is available for download in PDF format.

© The Ukrainian Biochemical Journal