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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)

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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
    CrossrefPubMedSearch in Google Scholar
  • 2 Böhm P, Dauber S, Baumeister L. Über Neuraminsäure, ihr Vorkommen und ihre Bedeutung im Serum. Klinische Wochenschrift 1954; 13: 289
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    Search in Google Scholar
  • 5 Dische Z. A new specific color reaction of hexuronic acids. Journal of Biological Chemistry 1947; 167: 189
    PubMedSearch in Google Scholar
  • 6 Elson L. A, Morgan W. T. J. A colorimetric method for determination of glucosamine and chondrosamine. Biochemical Journal 1933; 27: 1824
    CrossrefPubMedSearch in Google Scholar
  • 7 Hershgold E. J. The subunit structure of Human factor VIII (antihemophilic factor). Federation Proceedings 1971; 30: 540
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    CrossrefPubMedSearch in Google Scholar
  • 14 Kuntz E, Arnold C. Die klinische Aktivitäts-Beurteilung der Lungentuberkulose. Stuttgart.: Georg Thieme; 1963: 58
    Search in 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
    PubMedSearch in Google 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
    CrossrefPubMedSearch in Google Scholar
  • 17 McKee P. A. Purification and electrophoretic analysis of human antihemophilic factor (Factor VIII). Federation Proceedings 1970; 29: 647
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google Scholar
  • 20 Radhakrishnamurthy B, Berenson G. S. Differential determination of glucosamine and galactosamine. Clínica chimica Acta 1964; 10: 562
    PubMedSearch in Google 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
    CrossrefPubMedSearch in Google Scholar
  • 22 Stibbe J, Hemker H. C, van Creveld S. The inactivation of factor VIII in Vitro. Thrombosis et Diathesis Haemorrhagica 1972; 27: 43
    PubMedSearch in Google 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
    CrossrefPubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google 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
    PubMedSearch in Google Scholar
  • 27 Wagner A. Über den diagnostischen Wert der Eiweiß gebundenen Hexosen. Klinische Wochenschrift 1960; 23: 1187
    PubMedSearch in Google Scholar
  • 28 Warren L. The thiobarbituric acid assay of sialic acids. Journal of Biological Chemistry 1959; 234: 1971
    PubMedSearch in Google 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
    CrossrefPubMedSearch in Google Scholar