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In the intrinsic pathway, factor X is activated by a complex consisting of activated factor IX, factor VIII, phospholipid and calcium ions. The contribution of each of this components has been estimated by recombination of purified human coagulation factors, and measurement of the initial rate of factor Xa formation using a spectrophoto- metric assay.  In the absence of phospholipid and factor VIII, factor X is activated at a low, but significant rate. Addition of either phospholipid or activated factor VIII stimulates the initial rate of this reaction 250 and 500 fold, respectively; addition of both cofactors stimulates more than 100,000 fold. The activation of factor VIII by factor Xa or by thrombin is essential for the stimulating effect of factor VIII. Factor VIII complex, containing both VIIIR:WF and VIII:C, and purified factor VIII:C behave identically in this system; purified factor VIIIR:WF does not influence the rate of factor Xa formation.  The same kinetic approach was used for the characterization of preparations of abnormal factor VIII, obtained from plasma of haemophilia A patients.

The Contribution Of Factor VIII In The Intrinsic Activation Of Human Factor X