Further studies on human testicular acid phosphatases.

Four acid phosphatases were separated by gel filtration on Sepharose 6B and subsequent chromatography on DE-52 cellulose from human homogenate. The enzymes differed from each other in substrate preference, Km-values, modifier characteristics and molecular weights. The evidence obtained confirms that also in the human testis acid phosphatases of multiple molecular forms are present. Some of these may be specific for the testicular tissue.