Kinetic properties of the activator complexes plasmin--staphylokinase and plasmin(ogen)--streptokinase in vitro.

I. Y. Sazonova, R. B. Aisina, L. I. Muhametova, S. D. Varfolomeyev

Research output: Contribution to journalArticle

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Abstract

Comparative kinetic and electrophoretic study of the interaction of plasminogen (PG) with equimolar concentrations of staphylokinase (SPK) and streptokinase (SK) at 4 and 37 degreesC showed that the PG--SK complex has fibrinolytic and esterase activities, whereas the PG--SPK complex was inactive. Both esterase and fibrinolytic activities were enhanced during the conversion of the PG--SPK complex to the complex of plasmin (PL) with SPK (PL--SPK) at 37 and 4 degreesC, while the PG--SK complex was rapidly converted to the PL--SK complex with higher esterase activity only at 37 degreesC. The catalytic efficiency of Z-Lys-pNP hydrolysis (kcat/Km) by the preformed PL--SPK complex was twofold lower than that in the case of the PL--SK complex. Incubation of the PL--SPK and PG--SK(PL--SK) complexes at 37 degreesC for 24 h was associated with the degradation of the proteins and with different kinetics of lowering of esterase, plasminogen activator, and fibrinolytic activities. The PL--SPK complex was considerably more stable than the PG--SK(PL--SK) complex; streptokinase degraded more rapidly than staphylokinase. Kinetics of lysis of fibrin clots by the two complexes were similar, but the efficiency of lysis of plasma clots by the PL--SPK complex was significantly higher than that in the case of the PG--SK(PL--SK) complex (at 0.03-1 microM). Probably, unlike streptokinase, staphylokinase which is less susceptible to degradation in the PL--SPK complex and is released from the triple complex alpha2-antiplasmin--PL--SPK, forms a potentially highly active new complex with free molecules of plasminogen in the plasma.

Original languageEnglish (US)
Pages (from-to)66-74
Number of pages9
JournalBiochemistry. Biokhimiia
Volume64
Issue number1
StatePublished - Jan 1 1999

Fingerprint

Streptokinase
Fibrinolysin
Kinetics
Plasminogen
Esterases
estropipate
Staphylococcus aureus auR protein
In Vitro Techniques
Plasmas
Degradation
Antifibrinolytic Agents
Plasminogen Activators
Fibrin
Proteolysis
Hydrolysis

Keywords

  • Activity
  • Electrophoresis
  • Fibrinolysis
  • Plasmin(ogen)-staphylokinase complex
  • Plasmin(ogen)-streptokinase complex
  • Stability

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Chemistry(all)

Cite this

Sazonova, I. Y., Aisina, R. B., Muhametova, L. I., & Varfolomeyev, S. D. (1999). Kinetic properties of the activator complexes plasmin--staphylokinase and plasmin(ogen)--streptokinase in vitro. Biochemistry. Biokhimiia, 64(1), 66-74.

Kinetic properties of the activator complexes plasmin--staphylokinase and plasmin(ogen)--streptokinase in vitro. / Sazonova, I. Y.; Aisina, R. B.; Muhametova, L. I.; Varfolomeyev, S. D.

In: Biochemistry. Biokhimiia, Vol. 64, No. 1, 01.01.1999, p. 66-74.

Research output: Contribution to journalArticle

Sazonova, IY, Aisina, RB, Muhametova, LI & Varfolomeyev, SD 1999, 'Kinetic properties of the activator complexes plasmin--staphylokinase and plasmin(ogen)--streptokinase in vitro.', Biochemistry. Biokhimiia, vol. 64, no. 1, pp. 66-74.
Sazonova, I. Y. ; Aisina, R. B. ; Muhametova, L. I. ; Varfolomeyev, S. D. / Kinetic properties of the activator complexes plasmin--staphylokinase and plasmin(ogen)--streptokinase in vitro. In: Biochemistry. Biokhimiia. 1999 ; Vol. 64, No. 1. pp. 66-74.
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AB - Comparative kinetic and electrophoretic study of the interaction of plasminogen (PG) with equimolar concentrations of staphylokinase (SPK) and streptokinase (SK) at 4 and 37 degreesC showed that the PG--SK complex has fibrinolytic and esterase activities, whereas the PG--SPK complex was inactive. Both esterase and fibrinolytic activities were enhanced during the conversion of the PG--SPK complex to the complex of plasmin (PL) with SPK (PL--SPK) at 37 and 4 degreesC, while the PG--SK complex was rapidly converted to the PL--SK complex with higher esterase activity only at 37 degreesC. The catalytic efficiency of Z-Lys-pNP hydrolysis (kcat/Km) by the preformed PL--SPK complex was twofold lower than that in the case of the PL--SK complex. Incubation of the PL--SPK and PG--SK(PL--SK) complexes at 37 degreesC for 24 h was associated with the degradation of the proteins and with different kinetics of lowering of esterase, plasminogen activator, and fibrinolytic activities. The PL--SPK complex was considerably more stable than the PG--SK(PL--SK) complex; streptokinase degraded more rapidly than staphylokinase. Kinetics of lysis of fibrin clots by the two complexes were similar, but the efficiency of lysis of plasma clots by the PL--SPK complex was significantly higher than that in the case of the PG--SK(PL--SK) complex (at 0.03-1 microM). Probably, unlike streptokinase, staphylokinase which is less susceptible to degradation in the PL--SPK complex and is released from the triple complex alpha2-antiplasmin--PL--SPK, forms a potentially highly active new complex with free molecules of plasminogen in the plasma.

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