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Letters in Peptide Science

, Volume 4, Issue 4–6, pp 497–502 | Cite as

Integration of human plasminogen or streptokinase into stable complexes with oxidoreductases and pyruvate kinase

  • Vitaly N. Nikandrov
  • Oleg N. Murashko
  • Galina V. Vorobyova
  • Nelly S. Pyzhova
  • Natalie V. Kvyatkovskaya
  • Oksana A. Bartalevich
Article
  • 25 Downloads

Summary

The formation of stable equimolar complexes of streptokinase or plasminogen with muscle lactate dehydrogenase or pyruvate kinase, heart mitochondrial malate dehydrogenase and hepatic catalase at pH 7.4, 3.0 and 10.0 was first detected by differential spectroscopy methods. All complexes, except those of plasminogen with dehydrogenases, were resistant to 6 M urea. Judging from circular dichroism spectra, tertiary and secondary structures were considerably changed in the complexes. These changes were significantly dependent upon the nature of interacting proteins; in some cases their structures were more ordered. NAD (but not NADH) hampered the formation of streptokinase complexes with dehydrogenases. The plasminogen-activating function of streptokinase and the ability of plasminogen to be activated by streptokinase in the complexes with oxidoreductases were essentially unchanged. Pyruvate kinase induced a moderate (by 35%) increase in the streptokinase activating function. It is assumed that the formation of complexes of streptokinase or plasminogen with enzymes may serve as a link in metabolic regulation and/or intercellular interactions.

Keywords

Plasminogen activation Protein interactions Secondary and tertiary structure 

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Copyright information

© Kluwer Academic Publishers 1997

Authors and Affiliations

  • Vitaly N. Nikandrov
    • 1
  • Oleg N. Murashko
    • 1
  • Galina V. Vorobyova
    • 1
  • Nelly S. Pyzhova
    • 1
  • Natalie V. Kvyatkovskaya
    • 1
  • Oksana A. Bartalevich
    • 1
  1. 1.Laboratory of BiochemistryByelorussian Research Institute of Epidemiology and MicrobiologyMinskBelarus

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