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Human factor V, purified from citrated plasma by a method recently described by us (Bolnuis et al 1979) was found to be slightly contaminated with α2-macroglobulin. A rabbit antiserum to this preparation, obtained by frequent subcutaneous immunization, showed factor V procoagulant neutralizing activity. Immune electrophoresis demonstrated precipitation lines with α2-macroglobulin. This contamination was succesfully removed from the factor V preparation by affinity chromatography with specific raboit anti human α2-macroglobulin bound to Sepharose 2B. The antiserum to the original, impure factor V preparation showed no more precipitation arcs after absorption with 3% normal plasma and ammonium sulphate precipitation of the complexes. Factor V procoagulant neutralizing activity titre was estimated 1: 8 (50% neutralization after 1 hour incubation at 37°C.) This antiserum was used for the following studies: 1. An inhibitor neutralization assay was developed for measuring antigenic activities of the factor V molecule. Antigen concentration in a range from 12.5-100% could be reliably measured. 2. Fab-fragments, obtained by papain digestion of the purified IgG (by protein A SePharose chromatography) were labeled with 125I by an immobilized lactoperoxidase metnod. These Fab-fragments fully retained their factor V procoagulant neutralizing activity. 125I-Fab-frag ments were used in specific binding studies to both non-activated and ADP and thrombin-activated human blood platelets.

Improved Purification Method Of Human Plasma Factor V And Applications Of A Rabbit Anti-Human Factor V Antibody