Download PDF
Thromb Haemost 1974; 31(02): 328-338
DOI: 10.1055/s-0038-1649167
Original Article
Schattauer GmbH

Studies on the Characterization of Factor VIII and a Co-factor VIII

M. M. P Paulssen
1   Department of Clinical biochemistry, St. Clara Hospital, Rotterdam, Netherlands
2   Central Animal Laboratory of the University of Nijmegen, Netherlands (Head: Dr. M. J. Dobbelaar)
,
H. L. M. A Vandenbussche-Scheffers
1   Department of Clinical biochemistry, St. Clara Hospital, Rotterdam, Netherlands
2   Central Animal Laboratory of the University of Nijmegen, Netherlands (Head: Dr. M. J. Dobbelaar)
,
P. B Spaan
1   Department of Clinical biochemistry, St. Clara Hospital, Rotterdam, Netherlands
2   Central Animal Laboratory of the University of Nijmegen, Netherlands (Head: Dr. M. J. Dobbelaar)
,
T de Jong
1   Department of Clinical biochemistry, St. Clara Hospital, Rotterdam, Netherlands
2   Central Animal Laboratory of the University of Nijmegen, Netherlands (Head: Dr. M. J. Dobbelaar)
,
M. C Planje
1   Department of Clinical biochemistry, St. Clara Hospital, Rotterdam, Netherlands
2   Central Animal Laboratory of the University of Nijmegen, Netherlands (Head: Dr. M. J. Dobbelaar)
› Author Affiliations
Further Information

Publication History

Received 29 May 1973

Accepted 16 January 1974

Publication Date:
29 June 2018 (online)

    Permissions and Reprints

Summary

Factor VIII occurs in the body in two different forms. In lymph factor VIII is bound to chylomicra. In plasma, factor VIII is bound to a protein.

After delipidation of chylomicra we obtained a glycoprotein with a high polysaccharide content and a molecular weight of approx. 160,000.

In plasma, factor VIII is attached to a protein which is present in normal concentrations in plasma of patients with haemophilia A and in serum (co-factor VIII).

This factor is deficient in both the plasma and the serum of patients with von Willebrand’s disease.

The binding between factor VIII and co-factor VIII is reversible.

Some properties of these two factors are described.

 

  • References

  • 1 Andrews P. Estimation of the molecular weights of proteins by sephadex gel-filtration. Biochemical Journal 1964; 91: 222
    CrossrefPubMedGoogle Scholar
  • 2 Böhm P, Dauber S, Baumeister L. Über Neuraminsäure, ihr Vorkommen und ihre Bedeutung im Serum. Klinische Wochenschrift 1954; 13: 289
    PubMedGoogle Scholar
  • 3 Brown W. V, Levy R. J, Frederickson D. S. Studies of the proteins in human plasma very low density lipoproteins. Journal of Biological chemistry 1969; 244: 5687
    PubMedGoogle Scholar
  • 4 Denson K. W. E, Biggs R. Laboratory Diagnosis. Tests of Clotting Functions and their Standaridization. In Biggs R. (ed.) Human Blood Coagulation, Haemostasis and Thrombosis. Oxford: Blackwell scientific Publications; 1972: 288
    Google Scholar
  • 5 Dische Z. A new specific color reaction of hexuronic acids. Journal of Biological Chemistry 1947; 167: 189
    PubMedGoogle Scholar
  • 6 Elson L. A, Morgan W. T. J. A colorimetric method for determination of glucosamine and chondrosamine. Biochemical Journal 1933; 27: 1824
    CrossrefPubMedGoogle Scholar
  • 7 Hershgold E. J. The subunit structure of Human factor VIII (antihemophilic factor). Federation Proceedings 1971; 30: 540
    PubMedGoogle Scholar
  • 8 Hershgold E. J, Davison A. M, Janszen M. E. Isolation and some chemical properties of human factor VIII (antihemophilic factor). Journal of Laboratory and Clinical Medicine 1971; a 77: 185
    PubMedGoogle Scholar
  • 9 Hershgold E. J, Davison A. M, Janszen M. E. Human factor VIII (antihemophilic factor); Activation and inactivation by phospholipases. Journal of Laboratory and Clinical Medicine 1971; b 77: 206
    PubMedGoogle Scholar
  • 10 Hoyer L. W. Immunologic studies of antihemophilic factor (A. H.F., factor VIII) III. Comparative binding properties of human and rabbit anti-A.H.F. Blood 1972; a 39: 481
    PubMedGoogle Scholar
  • 11 Hoyer L. W. Immunologic studies of antihemophilic factor (A.H.F., factor VIII) Radioimmuno assay of A.H.F. antigen. Journal of Laboratory and Clinical Medicine 1972; b 80: 822
    PubMedGoogle Scholar
  • 12 Johnson A. J, Newman J, Howell M. B, Puszkin S. Purification of antihemophilic factor (A.H.F.) for clinical and experimental use. Thrombosis et Diathesis Haemorrhagica 1967; suppl 26: 377
    PubMedGoogle Scholar
  • 13 Kass L, Ratnoff O. D, Leon M. A. Studies on the purification of anti-hemophilic factor (factor VIII)I. Precipitation of antihemophilic factor by concanavalin A. Journal of Clinical Investigation 1969; 48: 351
    CrossrefPubMedGoogle Scholar
  • 14 Kuntz E, Arnold C. Die klinische Aktivitäts-Beurteilung der Lungentuberkulose. Stuttgart.: Georg Thieme; 1963: 58
    Google Scholar
  • 15 Lowry O. H, Rosebrough N. J, Fare A. L, Randall R. J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951; 23: 265
    PubMedGoogle Scholar
  • 16 Marchesi S. L, Shulman N. R, Gralnick H. R. Studies on the Purification and characterization of human factor VIII. Journal of Clinical Investigation 1972; 51: 2151
    CrossrefPubMedGoogle Scholar
  • 17 McKee P. A. Purification and electrophoretic analysis of human antihemophilic factor (Factor VIII). Federation Proceedings 1970; 29: 647
    PubMedGoogle Scholar
  • 18 Melani F, Bartelt K. M, Conrads R, Pfeiffer E. F. Die Jod 131-Mar-kierung von Insulin. ACTH und STH mit hoher spezifischer Aktivität zur Anwendung in der radio-immunologischen Methode. Zeitschrift für Klinische Chemie 1966; 4: 189
    PubMedGoogle Scholar
  • 19 Paulssen M. M. P, Wouterlood A. C. M. G. B, Scheffers H. L. M. A. Purification of the antihemophilic factor by gel filtration on agarose. Thrombosis et Diathesis Haemorrhagica 1969; 22: 577
    PubMedGoogle Scholar
  • 20 Radhakrishnamurthy B, Berenson G. S. Differential determination of glucosamine and galactosamine. Clínica chimica Acta 1964; 10: 562
    PubMedGoogle Scholar
  • 21 Ratnoff O. D, Kass L, Lang P. D. Studies on the purification of anti-hemophilic factor (Factor VIII). Journal of Clinical Investigation 1969; 48: 957
    CrossrefPubMedGoogle Scholar
  • 22 Stibbe J, Hemker H. C, van Creveld S. The inactivation of factor VIII in Vitro. Thrombosis et Diathesis Haemorrhagica 1972; 27: 43
    PubMedGoogle Scholar
  • 23 Stites D. P, Hershgold E. J, Perlman J. D. Factor VIII detection by hemagglutination inhibition: Hemophilic A and von-Willebrand’s disease. Science 1971; 171: 196
    CrossrefPubMedGoogle Scholar
  • 24 Van MoUrik J. A, Mochtar J. A. Purification of human antihemophilic factor (factor VIII) by gel chromatography. Biochemica et Biophisica Acta 1970; 221: 677
    PubMedGoogle Scholar
  • 25 Veltkamp J. J, Drion E. F, Loeliger E. A. Detection of the Carrier State in Heriditary Coagulation Disorders. Thrombosis et Diathesis Haemorrhagica 1968; 19: 279
    PubMedGoogle Scholar
  • 26 Veltkamp J. J, Sohalm S. W, Draaijer B, van de Torren K, Terpstra J. L. Levertransplantatie bij honden met ernstige Haemophilie A. 12e Federatieve Vergadering, Rotterdam 22-24 april 1971; 1971: 350
    PubMedGoogle Scholar
  • 27 Wagner A. Über den diagnostischen Wert der Eiweiß gebundenen Hexosen. Klinische Wochenschrift 1960; 23: 1187
    PubMedGoogle Scholar
  • 28 Warren L. The thiobarbituric acid assay of sialic acids. Journal of Biological Chemistry 1959; 234: 1971
    PubMedGoogle Scholar
  • 29 Zimmerman T. S, Ratnoff O. D, Powell A. E. Immunologic differentiation of classic hemophilia (factor VIII deficiency) and von Willebrand’s disease. Journal of Clinical Investigation 1971; 50: 244
    CrossrefPubMedGoogle Scholar