Purification of human prostatic acid phosphatase and preparation of a specific antiserum in the rabbit

A modification of previously described methods for the purification of human prostatic acid phosphatase from prostatic tissue is proposed. The purification scheme comprises an Ammonium sulphate fractionation and affinity chromatography on Concanavalin A-Sepharose after dialysis against water. After DEAE-Sephadex A 50 chromatography, the final step is an Ultrogel AcA 34 fractionation. The purified PAP has a specific enzymatic activity of 675 U/mg protein and the total yield is of 32%.