Thromb Haemost 1972; 27(03): 634-643
DOI: 10.1055/s-0038-1649402
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Measurement of Fibrin Proteolysis In Vivo by a Radioactive Fibrin-Millipore Tube Technique

R. W Cihak
1   Department of Pathology, Harbor General Hospital, Torrance, California
,
S. T Shaw Jr.
1   Department of Pathology, Harbor General Hospital, Torrance, California
› Author Affiliations
Further Information

Publication History

Publication Date:
24 July 2018 (online)

Summary

Millipore tubes containing radioactive fibrin can be used to measure fibrin proteolysis. Experiments described herein indicate that loss of soluble radioactivity from fibrin- containing tubes during in vivo incubation can be used to measure relative rates of lytic activity at specific locations within an organism under various conditions.

Preparation of urea-insoluble 125I-fibrin and its apparent purity and uniformity of label have been described. This preparation has been shown to be stable over a period of several months, when properly stored, in its response to protease activity and lack of spontaneous degradation. Contained within Millipore tubes, the fibrin is protected from direct cellular attack while it is susceptible to enzymes from the environment which can enter the porous chambers. Enzymatic degradation of fibrin releases diffusible radioiodinated peptides from the tubes. Thus, determination of fibrin-tube radioactivity before and following in vivo incubation may be used as a measurement of proteolytic rate within the organism.

This investigation was supported by a grant from the Ford Foundation


* Current Address : Atomic Bomb Casualty Commission U. S. Marine Corp. Air Station FPO, Seattle, Washington 98764


** Current Address: Department of Obstetrics and Gynecology; Los Angeles County/University of Southern California Medical Center; Los Angeles, California 90033.


 
  • References

  • 1 Shaw S. T, Cihak R. W, Moyer D. L. Fibrin Proteolysis in the Monkey Uterus: Variations With and Without IUD. Nature 228: 1097 1970;
  • 2 Blix S. Studies on the Fibrinolytic System in the Euglobulin Fraction of Human Plasma. Scand. J. clin. Lab. Invest 13 (Suppl. 58) 3 1961;
  • 3 Hunter W. M, Greenwood F. C. Preparation of Iodine-131 Labelled Human Growth Hormone of High Specific Activity. Nature 194: 495 1962;
  • 4 Lassen M. Heat Denaturation of Plasminogen in the Fibrin Plate Method. Acta phys. scand 27: 371 1952;
  • 5 Keller H. U, Sorlcin E. Studies on Chemotaxis. IX. Migration of Rabbit Leukocytes Through Filter Membranes. Proc. Soc. exp. Biol. (N. Y) 126: 677 1967;
  • 6 Ferry J. D, Morrison P. B. Preparation and Properties of Serum and Plasma Proteins. VIII. The Conversion of Human Fibrinogen to Fibrin Under Various Conditions. J. Amer, ehem. Soc 69: 388 1947;
  • 7 Morrison P. R. Preparation and Properties of Serum and Plasma Proteins. XV. Some Factors Influencing the Quantitative Determination of Fibrinogen. J. Amer. chem. Soc 69: 2723 1947;
  • 8 Bickford A. F, Sokolow M. Fibrinolysis as Related to the Urea Solubility of Fibrin. Thrombos. Diathes. haemorrh. (Stuttg) 05: 480 1961;
  • 9 Gormsen J, Fletcher A. P, Alkjaersig N, Sherry S. Enzymic Lysis of Plasma Clots : The Influence of Fibrin Stabilization on Lysis Rates. Arch. Biochem 120: 654 1967;
  • 10 Biddle J. M, Barnhart M. I. Ultrastructural Study of Fibrin Dissolution via Emigrated Polymorphonuclear Leukocytes. Amer. J. Pathol 45: 805 1964;
  • 11 Barnhart M. I. Importance of Neutrophilic Leukocytes in the Resolution of Fibrin. Fed. Proc 24: 846 1965;
  • 12 Gans H, Subramanian V, Tan B. H. Selective Phagocytosis : A New Concept in Protein Catabolism. Science 159: 107 1968;
  • 13 Walsh B. T, Barnhart M. I. Clearance of Coagulation and Fibrinolysis Products by the Reticuloendothelial System. Thrombos. Diathes. haemorrh. (Stuttg.) Suppl 36: 83 1969;