Thromb Haemost 1969; 21(02): 217-222
DOI: 10.1055/s-0038-1653530
Originalarbeiten - Original Articles - Travaux Originaux
Schattauer GmbH

Studies on Tissue Thromboplastin - Its Splitting into Two Separable Parts

M Hvatum
1   The Department of Microbiology, Dental Faculty, University of Oslo, Blindern, Norway
,
H Prydz
1   The Department of Microbiology, Dental Faculty, University of Oslo, Blindern, Norway
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Publikationsdatum:
10. Juni 2018 (online)

Summary

1. Sodium deoxycholate (DOC) splits tissue thromboplastin into two inactive parts, fraction A and fraction B, separable by gel filtration in the presence of DOC.

2. By recombination and subsequent removal of the DOC, the fractions reaggregate and regain full thromboplastic activity.

3. Fraction A consists mainly of protein, while phospholipid is the main constituent of fraction B.

 
  • References

  • 1 Hvatum M, Prydz H. Studies on tissue thromboplastin. I. Solubilization with sodium deoxycholate. Biochim. biophys. Acta (Amst) 130: 92 1966;
  • 2 Lowry O. H, Rosebrough N. J, Farr A. L, Randall R. J. Protein measurement with the Folin phenol reagent. J. biol. Chem 193: 265 1951;
  • 3 Chen Jr P. S, Toribara T. Y, Warner H. Microdetermination of phosphorus. Anal. Chem. (Wash) 28: 1756 1956;
  • 4 Âtland S, Hvatum M, Prydz H. Inactivation of Tissue Thromboplastin by Ultraviolet Irradiation. Thrombos. Diathes. haemorrh. (Stuttg) 19: 221 1968;
  • 5 To be reported later.
  • 6 Hvatum M, Hovig T, Prydz H. Studies on Tissue Thromboplastin - Electron Micrography. Thrombos. Diathes. haemorrh. (Stuttg) 21: 223 1969;
  • 7 Bangham A. D, Horne B. W. Negative Staining of Phospholipids and their Structural Modification by Surface-active Agents as observed in the Electron Microscope. J. molec. Biol 08: 660 1964;
  • 8 Hjort P, Bapaport S. I, Owren P. A. A Simple Specific One-Stage Prothrombin Assay, Using Russel’s Viper Venom in Cephalin Suspension. J. Lab. clin. Med 46: 89 1955;
  • 9 Griddle B. S, Edwards D. L, Petersen T. G. Chemical Studies on the Homogeneity of the Structural Protein from Mitochondria. Biochem. (Easton, Pa) 05: 578 1966;
  • 10 Bakerman S, Wasemiller G. Studies on Structural Units of Human Erythrocyte Membrane. I. Separation, Isolation, and Partial Characterization. Biochem. (Easton, Pa) 06: 1100 1967;
  • 11 Griddle B. S, Bock B. M, Green D. E, Tisdale H. Physical Characteristics of Proteins of the Electron Transfer System and Interpretation of the Structure of the Mitochondrion. Biochem. (Easton, Pa) 01: 827 1962;
  • 12 Deutsch 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;
  • 13 Stormorken H. Species differences of clotting factors in ox, dog, horse and man. Thromboplastin and proconvertin. Acta physiol, scand 41: 301 1957;
  • 14 Irsigler K, Lechner K, Deutsch E, Lomoschitz H. Studies on Tissue Thromboplastin. I. Species Specificity. Thrombos. Diathes. haemorrh. (Stuttg) 14: 18 1965;
  • 15 Hecht E, Oosterbaan van Lit W. L. Über die chemische Natur des Thromboplastins aus menschlicher Hirnsubstanz. Thrombos. Diathes. haemorrh. (Stuttg) 18: 223 1967;
  • 16 Hecht E. Chemical Nature of human Brain Thromboplastins. Nature (Lond) 214: 197 1967;
  • 17 Nemerson Y, Spaet T. H. The Activation of Factor X by Extracts of Rabbit Brain. Blood 23: 657 1964;