10
Views
47
CrossRef citations to date
0
Altmetric
Original Article

Rate of Activation and Electrophoretic Mobility of Unmodified and Partially Degraded Plasminogen Effects of 6-Aminohexanoic Acid and Related Compounds

&
Pages 167-176 | Received 02 Feb 1974, Accepted 28 May 1974, Published online: 28 Aug 2009

References

  • Abiko Y., Iwamoto M. Plasminogen‐plasmin system VII. Potentiation of antifibrinolytic action of a synthetic inhibitor, tranexamic acid, by α2‐macroglobulin antiplasmin. Biochim. biophys. Acta (Amst.) 1970; 214: 411
  • Abiko Y., Iwamoto M., Tomikawa M. Plasminogen‐plasmin system. V. A stoichiometric equilibrium complex of plasminogen and a synthetic inhibitor. Biochim. biophys. Acta (Amst.) 1969; 185: 424
  • Alkjaersig N. The purification and properties of human plasminogen. Biochem. J. 1964; 93: 171
  • Brockway W. J., Castellino F. J. The mechanism of the inhibition of plasmin activity by ϵ‐aminocaproic acid. J. biol. Chan. 1971; 246: 4641
  • Brockway W. J., Castellino F. I. Measurement of the binding of antifibrinolytic amino acids to various plasminogens. Arch. Biochem. 1972; 151: 194
  • Castellino F. J., Brockway W. J., Thomas J. K., Liao H. Rotational diffusion analysis of the conformational alterations produced in plasminogen by certain antifibrinolytic amino acids. Biochemistry 1973; 12: 2787
  • Claeys H., Molla A., Verstraete M. Digestion of human plasminogen by human plasmin. Proceedings of the Fourth International Congress on Thrombosis and Haemostasis, Vienna, June, 19–221973, Abstract 153
  • Dsutsch D. G., Mertz E. T. Plasminogen: purification from human plasma by affinity chromatography. Science 1970; 170: 1095
  • Egeblad K. Effects of epsilon‐aminocaproic acid on fibrin clot lysis. Thrombos. Diathes. haemorrh. (Stuttg.) 1966; 15: 173
  • Ganrot P. O. On the determination of molar concentrations of plasmin and plasmin inhibitors. Acta chem. scand. 1957; 21: 595
  • Ganrot P. O. Crossed immunoelectrophoresis. Scand. J. clin. Lab. Invest. 1972; 29(Suppl. 124)39
  • Johansson B. G. Agarose gel electrophoresis. Scand. J. clin. Lab. Invest. 1972; 29(Suppl. 124)7
  • Kok P., Astrup T. Isolation and purification of a tissue plasminogen activator and its comparison with urokinase. Biochemistry 1969; 8: 79
  • Lorand L., Condit E. V. Ester hydrolysis by urokinase. Biochemistry 1955; 4: 265
  • McDonagh J., Messel H., McDonagh R. P., Jr., Murano G., Blombäck B. Molecular weight analysis of fibrinogen and fibrin chains by an improved sodium dodecyl sulphate gel electrophoresis method. Biochim. biophys. Acta (Amst.) 1972; 257: 135
  • Müllertz S. Formation and properties of the activator of plasminogen and of human and bovine plasmin. Biochem. J. 1955; 61: 424
  • Müllertz S. Molecular forms of plasmin and protease inhibitors in human fibrinolytic postmortem plasma. Scand. J. clin. Lab. Invest. 1972; 30: 369
  • Nilsson I. M. Blödnings‐ och Thrombossjukdomar. Bohusläningens AB, UddevallaSweden 1971
  • Rickli E. E., Otavsky W. I. Release of an N‐terminal peptide from human plasminogen during activation with urokinase. Biochim. biophys. Acta (Amst.) 1973; 295: 381
  • Robbins K. C., Summaria L., Hsieh B., Shah R. J. The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin. J. biol. Chem. 1967; 247: 2333
  • Sjöholm I., Wiman B., Wallén P. Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6‐aminohexanoic acid. Europ. J. Biochem. 1973; 39: 471
  • Summaria L., Arzadon L., Bernabe P., Robbins K. C., Barlow G. H. Characterization of the NH2‐terminal glutamic acid and NH2‐terminal lysine forms of human plasminogen isolated by affinity chromatography and isoelectric focusing methods. J. biol. Chem. 1973; 248: 2984
  • Thorsen S., Astrup T. Substrate composition and the effect of ϵ‐aminocaproic acid on tissue plasminogen activator and urokinase‐induced fibrinolysis. Thrombos. Diathes. haemorrh. (Stuttg.)
  • Thorsen S., Kok P., Astrup T. Molecular alterations of plasminogen disclosed by the effects of ϵ‐aminocaproic acid (ϵACA) on fibrinolysis and caseinolysis induced by urokinase (UK). Fed. Proc. 1972; 31, Abstract 106
  • Thorsen S., Kok P., Astrup T. Reversible and irreversible alterations of human plasminogen indicated by changes in susceptibility to plasminogen activators and in response to ϵ‐aminocaproic acid. Thrombos. Diathes. haemorrh. (Stuttg.)
  • Wallén P., Wiman B. Characterization of human plasminogen. I. On the relationship between different molecular forms of plasminogen demonstrated in plasma and found in purified preparations. Biochim. biophys. Acta (Amst.) 1970; 221: 20
  • Wallén P., Wiman B. Characterization of human plasminogen. II. Separation and partial characterization of different molecular forms of human plasminogen. Biochim. biophys. Acta (Amst.) 1972; 257: 122
  • Wallén P., Wiman B. On the formation and properties of an intermediate form of human plasminogen generated during activation with urokinase. Proceedings of the Fourth International Congress on Thrombosis and Haemostasis, Vienna, June, 19–221973, Abstract 150
  • Walton P. L. The hydrolysis of α‐N‐acetylglycyl, L‐lysine methyl ester by urokinase. Biochim. biophys. Acta (Amst.) 1967; 132: 104
  • White W. F., Barlow G. H. Methods in Enzymology, G. E. Perlmann, L. Lorand. Academic Press, New York and London 1970; vol. 19: 665–672
  • Wiman B., Wallén P. Activation of human plasminogen by an insoluble derivative of urokinase. Europ. J. Biochem. 1973; 36: 25

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.