Purification of antibody to galactosyl-protein conjugates.

A rapid procedure for purification of rabbit antibody to beta-D-galacto-sylphenylazo-bovine serum albumin is described. Antibody was precipitated with a heterologous antigen and was then dissociated from the precipitated complex with hapten. The antigen was partially removed by pH adjustment, and antibody was separated from residual antigen and from hapten by partition chromatography on Sephadex G-25. The antibody, obtained in 50 to 55 percent over-all yield, was 96 percent reactive with homologous antigen. It appeared to consist, of 95 percent of a single component, based upon physicochemical measurements.