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...

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Main Author: E. I. Yusova
Format: Article
Language:English
Published: National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry 2014-06-01
Series:Biotechnologia Acta
Subjects:
Online Access:http://biotechnology.kiev.ua/images/storage/3_2014/yusova.pdf
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author E. I. Yusova
author_facet E. I. Yusova
author_sort E. I. Yusova
collection DOAJ
description 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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spelling doaj.art-afd00e5b3b114e7a9192bc45efac160f2023-09-02T00:49:04ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryBiotechnologia Acta2410-77512410-776X2014-06-0173334210.15407/biotech7.03.033PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECTE. I. Yusova0Palladian Biochemistry Institute of the National Academy of Sciences of Ukraine, KyivThe 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.http://biotechnology.kiev.ua/images/storage/3_2014/yusova.pdfstreptokinase36 kDa-streptokinase fragmentfibrin
spellingShingle E. I. Yusova
PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
Biotechnologia Acta
streptokinase
36 kDa-streptokinase fragment
fibrin
title PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
title_full PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
title_fullStr PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
title_full_unstemmed PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
title_short PLASMINOGEN ACTIVATION BY LOW MOLECULAR WEIGHT STREPTOKINASE AND FIBRIN EFFECT
title_sort plasminogen activation by low molecular weight streptokinase and fibrin effect
topic streptokinase
36 kDa-streptokinase fragment
fibrin
url http://biotechnology.kiev.ua/images/storage/3_2014/yusova.pdf
work_keys_str_mv AT eiyusova plasminogenactivationbylowmolecularweightstreptokinaseandfibrineffect