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Thromb Haemost 1977; 38(01): 344
DOI: 10.1055/s-0039-1682495
Poster Session I
Schattauer GmbH

Degradation of Factor VIII-Related Protein in Factor VIII Concentrates

T. Jakab
1   Hematology Laboratory, Inselspital, and Central Laboratory, Transfusion Service, Swiss Red Cross, Berne, Switzerland
,
R. Pflugshaupt
1   Hematology Laboratory, Inselspital, and Central Laboratory, Transfusion Service, Swiss Red Cross, Berne, Switzerland
,
M. Furlan
1   Hematology Laboratory, Inselspital, and Central Laboratory, Transfusion Service, Swiss Red Cross, Berne, Switzerland
,
E.A. Beck
1   Hematology Laboratory, Inselspital, and Central Laboratory, Transfusion Service, Swiss Red Cross, Berne, Switzerland
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Publication Date:
16 April 2019 (online)

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Lipolytic and/or proteolytic treatment of highly purified human factor VIII results in a progressive disappearance of high-molecular weight protein as shown by electrophoresis on 3% Polyacrylamide gels in the presence of sodium dodecyl sulphate. Partial degradation of factor VIII is typically accompanied by a relative increase of factor VIII-related antigen (VIII R:AG)whereas coagulant activity (VIII:C) or von Willebrand activity (VIII R:WF) may still appear intact. VIII R:AG was measured by crossed Immunoelectrophoresis against specific heterologous antibody in agarose gels. VIII R:WF was expressed as ristocetin cofactor activity in comparison with a normal plasma pool. Assuming a VIII R:AG/ VIII R:WF ratio of 1.0 in our normal plasma, we found a similar ratio using intact purified factor VIII. This ratio increased regularly following proteolytic degradation of factor VIII concentrate by contaminating proteases or plasmin. Our findings suggest that a high VIII R:AG/VIII R:WF ratio could indicate undesirable alterations of VIII-related protein(s) during plasma fractionation.