PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
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..
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2014 |
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| Erschienen: |
2014 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:7 |
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| Enthalten in: |
Biotechnologia Acta - 7(2014), 3, Seite 33-42 |
| Sprache: |
Englisch ; Russisch ; Ukrainisch |
|---|
| Beteiligte Personen: |
E. I. Yusova [VerfasserIn] |
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| Links: |
doi.org [kostenfrei] |
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| Themen: |
36 kDa-streptokinase fragment |
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| doi: |
10.15407/biotech7.03.033 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
DOAJ004195884 |
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| 520 | |a 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. | ||
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