Thromb Haemost 1976; 36(01): 090-103
DOI: 10.1055/s-0038-1648013
Original Article
Schattauer GmbH

Properties of Human Tissue Thromboplastins from Brain, Lung, Arteries, and Placenta

H Gonmori
1   Department of Medicine, University of Colorado, School of Medicine, Denver, Colorado 80220
,
Y Takeda
1   Department of Medicine, University of Colorado, School of Medicine, Denver, Colorado 80220
› Author Affiliations
Further Information

Publication History

Received 30 September 1975

Accepted 20 March 1976

Publication Date:
03 July 2018 (online)

Summary

Properties of purified and delipidated human tissue thromboplastins (TTPs) from brain (BTTP), lung (LTTP), arteries (ATTP) and placenta (PTTP) were studied. The extinction coefficients were closely similar with a mean value of 8.3 ± 0.01 (SD). The molecular weights were 200,000 ± 3,000 (SD) (BTTP), 90,000 ± 2,000 (SD) (LTTP), 110,000 ± 3,000 (SD) (ATTP) and 250,000 ± 4,000 (SD) (PTTP). The maximum activity of each delipidated TTP after relipidation was obtained when phospholipid-delipidated TTP ratio was 2.0, and the maximum specific activity was 440 units per mg BTTP, 270 units per mg LTTP, 80 units per mg ATTP and 600 units per mg PTTP. Ouchterlony analysis with anti-delipidated PTTP antibody showed the reaction of partial identity between delipidated TTPs and the antibody. Studies of the reactivity of I-125-delipidated TTPs with the antibody gave the following average values for % bound I-125-TTPs in 2 hours: 3.6± 0.2 (SD) % (I-125-BTTP), 11.0± 0.3 (SD) % (I-125-LTTP), 4.4±0.2 (SD) % (I-125-ATTP) and 13.7±0.3 (SD) % (I-125-PTTP). It was also found that the antibody markedly neutralized the coagulant activity of saline extracts of brain, lung and placenta. These results indicate that delipidated BTTP, LTTP, ATTP and PTTP are different while being similar in some aspects and that complete TTPs are not coated with lipids in a manner inaccessible to anti-delipidated PTTP antibody.

 
  • References

  • 1 Andrews P. 1965; The gel-filtration behavior of proteins related to their molecular weights over a wide range. Biochemical Journal 96: 595.
  • 2 Astrup T, Albrechtsen O. K, Claassen M, Rasmussen J. 1959; Thromboplastic and fibrinolytic activity of the human aorta. Circulation Research 7: 969.
  • 3 Astrup T, Buluk K. 1963; Thromboplastic and fibrinolytic activities in vessels of animals. Circulation Research 13: 253.
  • 4 Biggs R. 1972. Human Blood Coagulation, Haemostasis and Thrombosis. Blackwell Scientific Publications; London, England: 593.
  • 5 Bjørklid E, Storm E, Prydz H. 1973; The protein component of human brain thromboplastin. Biochemical and Biophysical Research Communications 55: 969.
  • 6 Chargaff E, Moore D. H, Benedich A. 1942; Ultracentrifugal isolation from lung tissue of a macromolecular protein component with thromboplastic properties. Journal of Biological Chemistry 145: 593.
  • 7 Cuatrecasas P. 1970; Protein purification by affinity chromatography. Journal of Biological Chemistry 245: 3059.
  • 8 Davis B. J. 1964; Disc electrophoresis. II. Methods and application to human serum proteins. Annals of New York Academy of Sciendes 121: 404.
  • 9 Deutsch E, Irsigler K, Lomoschitz H. 1964; Studien über Gewebethromboplastin. I. Reinigung, chemische Charakterisierung und Trennung in Eiweiß- und Lipoidenteil. Thrombosis et Diathesis Haemorrhagica 12: 12.
  • 10 Gonmori H, Takeda Y. 1975; Properties of canine tissue thromboplastins from brain, lung, arteries and veins. American Journal of Physiology 229: 618.
  • 11 Hardaway R. M. 1966. Syndromes of Disseminated Intravascular Coagulation. Charles C. Thomas Publisher; Springfield, Illinois: 133.
  • 12 Hecht E. R, Cho M. H, Seegers W. H. 1958; Thromboplastin: Nomenclature and preparation of protein-free material different from platelet factor 3 or lipid activator. American Journal of Physiology 193: 584.
  • 13 Hvatum M, Prydz H. 1969; Studies on tissue thromboplastin. Its splitting into two separate parts. Thrombosis et Diathesis Haemorrhagica 21: 217.
  • 14 Lanchantin G. F, Ware R. G. 1953; Identification of a thromboplastin inhibitor in serum and in plasma. The Journal of Clinical Investigation 32: 381.
  • 15 Laurell C. B. 1966; Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Analytical Biochemistry 15: 45.
  • 16 McFarlane A. S. 1958; Efficient tracer labelling of proteins with iodine. Nature (London) 182: 53.
  • 17 McKay D. G, Wahle G. J. 1955; Disseminated thrombosis in colon cancer. Cancer 8: 970.
  • 18 Nemerson Y. 1968; The phospholipid requirement of tissue factor in blood coagulation. The Journal of Clinical Investigation 47: 72.
  • 19 Nemerson Y. 1969; Characteristics and lipid requirements of coagulant proteins extracted from lung and brain: The specificity of the protein component of tissue factor. The Journal of Clinical Investigation 48: 322.
  • 20 Takeda Y. 1970; Studies of the effects of heparin, coumadin and vitamin K on prothrombin metabolism and distribution in calves with the use of I-125-prothrombin. Characterization of the prothrombin system. The Journal of Laboratory and Clinical Medicine 75: 355.
  • 21 Taxeda Y. 1972; Studies of the metabolism and distribution of prothrombin in healthy men with homologous I-125-prothrombin. Thrombosis et Diathesis Haemorrhagica, 2 7: 472.
  • 22 Taxeda Y, Naxabayashi M. 1974; Physicochemical and biological properties of human and canine plasmins. The Journal of Clinical Investigation 53: 154.
  • 23 Tocantins L. M. 1943; Demonstration of antithromboplastic activity in normal and hemophilic plasma. American Journal of Physiology 139: 265.
  • 24 Weber K, Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244: 4406.
  • 25 Wide L. 1969; Radioimmunoassays employing immunosorbents. Acta Endocrinologica, (Supplement) 63: 207.
  • 26 Williams W. J. 1966; The activity of human placenta microsomes and brain particles in blood coagulation. Journal of Biological Chemistry 241: 1840.