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Home Archive 2014 № 3 PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT E. I. Yusova
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ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)

Biotechnologia Acta
V. 7, No 3, 2014


"Biotechnologia Acta" v. 7, no 3, 2014
doi: 10.15407/biotech7.03.033
Р. 33-42, Bibliography 38, Russian.
Universal Decimal classification: 577.151.4

PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT

E. I. Yusova

Palladian Biochemistry Institute of the National Academy of Sciences of Ukraine, Kyiv

The purpose is to study the plasminogen-activating activity of 36 kDa-streptokinase fragment, influences of desAB-fibrin on this process and low molecular weight streptokinase on plasmin catalytic properties as well.

The 36 kDa-fragment lacking the 63 N- and 34 C-terminal amino acid residues was obtained by preparative electrophoresis from chymotrypsin hydrolyzate of the native streptokinase. It was shown that 36 kDa streptokinase activates Glu-plasminogen in solution only at high concentrations of reacting components (2•10-7M). Activation process begins after a long lag-period and is in 100 times slower compared with the native streptokinase. Lys-plasminogen, mini-plasminogen (Val442-plasminogen) but not its Glu-form are activated at definitely lower protein concentrations (5•10-8M), while the reaction rate with mini-plasminogen is order of magnitude greater as compared with Lys-plasminogen and is equal  to 4,3•10-2 and 5•10-3 o.u./min respectively. DesAB-fibrin increases efficiently the rate of Glu- and Lys- plasminogen activation by 36 kDa-streptokinase and practically has no effect on the rate of mini-plasminogen activation. Low molecular weight streptokinase has no influence on amidase and fibrinolytic activity of plasmin and does not protect the enzyme from inhibitory effect of α2-antiplasmin. In the presence of the streptokinase fragment, plasmin showed no its activator activity towards plasminogen.

A  conclusion is made, that during plasminogen activation by low molecular weight streptokinase in the presence of desAB fibrin, a certain site of the fibrin molecule acts as N-terminal peptide of the native streptokinase, inducing conformational changes in proenzyme. These changes are necessary for quick complex formation with 36- kDa streptokinase and formation of the active centre in proenzyme molecule by this form of streptokinase.

Key words: streptokinase, 36 kDa-streptokinase fragment, plasminogen, fibrin.

© Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, 2008

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Home Archive 2014 № 3 PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT E. I. Yusova

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