第VIII因子とコラーゲンの相互関係

抄録

Factor VIII complex bound to both collagen in suspension and collagen coupled Sepharose beads with preferential binding of the forms of FVIIIR: Ag with the FVIIIR: RCoF. The FVIIIR: Ag in the eluate from collagen affinity column showed less anodal migration in crossed immunoelectrophoresis compared to the FVIIIR: Ag in the breakthrough fractions, suggesting the presence of higher molecular weight forms of FVIIIR: Ag in the eluate.
The new immunoelectrophoretic methods were described for studying the interaction between collagen and FVIIIR: Ag. Affinity immunoelectrophoresis with a collagen wedge revealed a different pattern of adsorption between FVIIIR: Ag in normal plasma and the FVIIIR: Ag in commercial FVIII preparations or in VWD IIa plasma. By the method of crossed affinity immunoelectrophoresis, most of the FVIIIR: Ag of normal plasma was adsorbed by the 100μg/ml collagen spacer gel, while no FVIIIR: Ag of variant VWD IIa plasma bound to the same concentration of collagen. Our methods of affinity immunoelectrophoresis with collagen spacer gel were easy to perform and may be useful for screening variant VWD plasmas. The use of an affinity wedge is a convenient method for finding quickly an optimal concentration of an affinity reagent.