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Thromb Haemost 1965; 14(01/02): 018-031
DOI: 10.1055/s-0038-1654851
Originalarbeiten — Original Articles — Travaux Originaux
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Studies on Tissue Thromboplastin II. Species Specificity*)[**)]

K Irsigler
1   First Medical Department, University of Vienna, (Head: Prof. Dr. E. Deutsch)
,
K Lechner
1   First Medical Department, University of Vienna, (Head: Prof. Dr. E. Deutsch)
,
E Deutsch
1   First Medical Department, University of Vienna, (Head: Prof. Dr. E. Deutsch)
,
with the technical assistence of H. Lomoschitz › Author AffiliationsThis work was supported from the National Heart Institute, National Institutes of Health, Bethesda, Md, USA under grant Nr. HE-06245.
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Publication History

Publication Date:
24 July 2018 (online)

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Summary

1. Purified brain tissue thromboplastins of human, bovine and chicken origin have been tested on homologous and heterologous plasmas.

2. Purified brain tissue thromboplastin is species specific.

3. Lipid extracts from purified brain tissue thromboplastin prepared with pyridin show a negligable residual species specificity, probably caused by a slight contamination with brain tissue thromboplastin.

4. The activity curves of our lipid extracts differ from typical curves expected for lipid activators by a less distinct inhibition in high concentrations probably caused by a different composition of petrol-ether and pyridin extracts.

5. The protein part of tissue thromboplastin does not activate prothrombin in any system.

6. The protein part of tissue thromboplastin of one species could be combined with the lipid part of another species to form an active tissue thromboplastin.

7. The species specificity of these combinations was determined by the source of protein used.

** Presented in part at the Xth Congress of the International Society of Haematology, Stockholm 1964.


 

  • References

  • 1 Bartlett G. E. Phosphorus Assay in Column Chromatography. J. biol. Chem. 234: 466 1959;
    PubMedGoogle Scholar
  • 2 Blombäck B. Chemical Aspects of Fibrinogen and Fibrin. In: Fibrinogen and Fibrin, Turnover of Clotting Factors. Suppl. ad. Thrombos. Diathes. haemorrh. (Stuttg) 1963
    PubMedGoogle Scholar
  • 3 Deutsah E, Irsigler K, Lomoschitz H. Studien über Gewebethromboplastin. 1. Reinigung, chemische Charakterisierung und Trennung in einen Eiweiß- und Lipoidanteil. Thrombos. Diathes. haemorrh. (Stuttg) 12: 12 1964;
    PubMedGoogle Scholar
  • 4 Hecht E. Studien über den lipoiden Aktivator der Blutgerinnung. Thrombos. Diathes. haemorrh. (Stuttg) 01: 380 1957;
    PubMedGoogle Scholar
  • 5 Mann F. D, Hum M. Co-thromboplastin, a probable Factor in Coagulation of Blood. Amer. J. Physiol. 164: 105 1951;
    PubMedGoogle Scholar
  • 6 Mann F. D, Hum M. Species Specifity of Thromboplastin. Proc. Soc. Biol. 79: 18 1952;
    PubMedGoogle Scholar
  • 7 Owen ChA, Hum M, Mann F. D. Dextran as a Substitute for Acacia in Assay of Plasma Prothrombin. Amer. J. clin. Path. 25: 1279 1955;
    PubMedGoogle Scholar
  • 8 Russel F, Doolittle R. F, Surgenor D. M. Blood Coagulation in Fish. Amer. J. Physiol. 203: 964 1962;
    PubMedGoogle Scholar
  • 9 Seegers W. H. The Purification of Prothrombin. Rec. Chem. Progr. 13: 143 1952;
    PubMedGoogle Scholar
  • 10 Vorlovâ Z, Starâ I, Deimlovâ E. Beitrag zur Spezifität der Thromboplastine. Proc. 8th Congr. Haemat. Vienna. II: 418 1961;
    PubMedGoogle Scholar
  • 11 Ware A. G, Seegers W. H. Two stage procedure for the quantitative determination of Prothrombin Concentration. Amer. J. clin. Path. 19: 471 1949;
    PubMedGoogle Scholar