Thromb Haemost 1969; 22(02): 240-250
DOI: 10.1055/s-0038-1651439
Originalarbeiten-Original Articles-Travaux Originaux
Schattauer GmbH

Diffusion Characteristics of Human Plasminogen(as Shown by Two Agar Diffusion Techniques)

R. J Stuckey
1   Senior Photographer, Department of Experimental Pathology, University of Birmingham
,
P Wolf M.D.
2   External Scientific Staff, Medical Besearch Council, attached to the Department of Experimental Pathology, University of Birmingham
› Author Affiliations
Further Information

Publication History

Publication Date:
10 June 2018 (online)

Summary

The relative diffusion rates of human plasminogen in agar has been compared with immune rabbit γ globulin and with streptokinase. A ratio of 1.1106 was found for plasminogen/immune rabbit γ globulin diffusion and a ratio of 0.80 for plasminogen/ streptokinase. These values were unaltered when plasminogen in normal fresh plasma and serum was replaced by three differently prepared plasminogen concentrates. Taking the D20 value for rabbit γ globulin as 4.23 × 10–7 cm2 sec−1 and for streptokinase the value of 6.1 × 10–7 cm2 sec–1, the corresponding values for human plasminogen were 4.7 and 4.9 × 10–7 cm2 sec–1. The widely divergent D20 values for human plasminogen and plasmin in the literature are reviewed and discussed.

 
  • References

  • 1 Allison A. C, Humphrey J. H. A theoretical and experimental analysis of double diffusion precipitin reactions in gels and its application to characterisation of antigens. Immunology 3: 95-106 1960;
  • 2 Blatt W. F, Segal H, Gray J. L. Purification of streptokinase and human plasmin and their interaction. Thrombos. Diathes. haemorrh. (Stuttg.) 11: 393-403 1964;
  • 3 Davies M. C, Englert M. E. Physical properties of highly purified human plasminogen. J. biol. Chem. 235: 1011-1013 1960;
  • 4 Davies M. C, Englert M. E, de Renzo E. C. Interaction of streptokinase on human plasminogen. J. biol. Chem. 239: 2651-2656 1964;
  • 5 Doleschel W, Auerswald W. Physico-chemical characterization of human gamma globulin subtraction capable of forming plasminogen activator with streptokinase. Med. Pharmacol. Exp. 14: 145-151 1966;
  • 6 Kabat E. A, Mayer M. M. Experimental immunochemistry. Second edition.. Charles C. Thomas; Springfield, Ill. (USA): 1961: 327.
  • 7 Lewis J. H. Separation and molecular weight estimation of coagulation and fibrinolytic proteins by sephadex gel filtration. Proc. Soc. exp. Biol. (N. Y.) 116: 120-122 1964;
  • 8 Neurath H. The Proteins. Second edition. Vol. Ill Academic Press; New York - London: 1965
  • 9 Robbins K. C, Summaria L, Elwyn D, Barlow G. H. Further studies on the purification and characterisation of human plasminogen and plasmin. J. biol. Chem. 240: 541-550 1965;
  • 10 Schulman S, Alkjaersig N, Sherry S. Physiochemical studies on human plasminogen and plasmin. J. biol. Chem. 233: 91-97 1958;
  • 11 Schultze H. E, Heremans J. F. Molecular Biology of Human Proteins. Vol. I. Elsevier Publishing Co.; Amsterdam — London — New York: 1966
  • 12 Wallen P, Bergström K. Purification of human plasminogen on DEAE-cellulose. Acta chem. scand. 14: 217-218 1960;
  • 13 White W. F, Barlow G. H, Mozen M. M. The isolation and characterisation of plasminogen activators (urokinase) from human urine. Biochemistry 5: 2160-2169 1966;
  • 14 Wolf P. Fibrinolytic activity and coronary-artery disease. Lancet I: 1312 1968;
  • 15 Wolf P. Modification of the fibrin agar plate for measurements of the components of the fibrinolytic system (I. The measurements of plasminogen on Type I fibrin agar plates). Thrombos. Diathes. haemorrh, (Stuttg.) 20: 50-65 1968;
  • 16 Wolf P. Modification of the fibrin agar plate for measurements of the components of the fibrinolytic system (II. Measurements of intrinsic plasminogen activator and its inhibitor on Type II fibrin agar plate). Thrombos. Diathes. haemorrh. (Stuttg.) 20: 66-77 1968;