Thromb Haemost 1968; 19(01/02): 145-160
DOI: 10.1055/s-0038-1651191
Originalarbeiten – Original Articles – Travaux Originaux
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Urokinase Activation of Plasminogen and Spontaneous Inactivation of the Plasmin Formed

A Kinetic Study
W Berg
1   Medical Department II, Sahlgrenska Hospital, University of Göteborg, Sweden
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Publication History

Publication Date:
27 June 2018 (online)

Summary

The kinetics of the activation of plasminogen into plasmin with urokinase and the inactivation rate of the plasmin formed are studied.

As a first order reaction is obtained with low plasminogen concentrations and a zero-order reaction is obtained with high concentrations, the activation seems to follow the Michaelis-Menten’s law. The reaction does not go to completion, however. Different activity levels, which are dependent on the urokinase concentration, can be observed.

The activation rate increases with temperature. A maximum can be seen at about 42° C.

Between 4° C and 15° C, the inactivation of the plasmin formed is minimal, but it increases rapidly at higher temperatures. The inactivation follows approximately a first order reaction with respect to time. If the plasminogen concentration is low, the over-all reaction will be that of two consecutive first order reactions.

 
  • References

  • 1 Alkjaersig N, Fletcher A.P, Sherry S. The activation of human plasminogen. J. biol. Chem. 1958; 233: 86
  • 2 Berg W. A method to correct for the continuing activation during the second stage in a two-stage assay Exemplified by the urokinase activation of plasminogen determined by the lysis time method. Thrombos. Diathes. haemorrh. (Stuttg.) 1967; 19: 161
  • 3 Berg W, Korsan-Bengtsen K. Separation of human fibrinogen and plasminogen by means of gel filtration. Thrombos. Diathes. haemorrh. (Stuttg.) 1963; 9: 151
  • 4 Berg W, Korsan-Bengtsen K, Ygge J. Plasminogen assay by means of the lysis time method. Thrombos. Diathes. haemorrh. (Stuttg.) 1965; 15: 127
  • 5 Berg W, Korsan-Bengtsen K, Ygge J. Preparation of human plasminogen suitable as substrate of quantitative determination of plasminogen activators. Thrombos. Diathes. haemorrh. (Stuttg.) 1966; 15: 11
  • 6 Berg W, Korsan-Bengtsen K, Ygge J. Human and bovine plasminogen-free thrombin, purified by means of gel filtration and ion exchange chromatography. Thrombos. Diathes. haemorrh. (Stuttg.) 1966; 15: 501
  • 7 Berg W, Korsan-Bengsten K, Ygge J. Theoretical basis and standardization of the one-stage lysis time method for determination of urokinase. Thrombos. Diathes. haemorrh. (Stuttg.) 1967; 19: 169
  • 8 Daniels F. Alberty: R.A. Physical chemistry. 2nd edition p. 310. John Wiley & Sons Inc. New York London 1962
  • 9 Kaplan W. Ordinary differential equations. Addison-Wesley publishing Company Inc. Reading. Palo Alto, London 1962
  • 10 Kjeldgaard N.O, Ploug J. Urokinase an activator of plasminogen from human urine. II Mechanism of plasminogen activation. Biochim. biophys. Acta (Amst.) 1957; 24: 283
  • 11 Kline D.L. Studies on the purification and activation of plasminogen (Profibrinolysin) Yale J. Biol. Med. 1954; 2 (05) 356
  • 12 Marcus G, Ambrus C.M. On the formation of different types of plasmin by streptokinase activation. J. biol. Chem. 1960; 235: 1673
  • 13 Marcus G, Werkheiser W.C. The interaction of streptokinase with plasminogen I Fractional properties of the activated enzyme. J. biol. Chem. 1964; 239: 2637
  • 14 Sgouris J.T. Taylor H.L. McCall: K.B. Urokinase activation of human plasminogen Abstr. 129th Meeting Am. chem. Soc. page 1956 13c
  • 15 Slotta K.H, Michl H, Santos B.G. Comparative studies on notive and acid-treated plasminogen. Biochim. biophys. Acta (Amst.) 1962; 58: 459