Acid phosphatase in the lysosomal and microsomal fractions of human prostatic epithelium.

Polyacrylamide gel electrophoresis of acid phosphatase from prostatic tissue reveals one more band than seminal plasma. It was attempted to ascertain which subcellular fraction was responsible for that intracellularly localized enzyme. Prostatic epithelium from patients with prostatic hyperplasia was homogenized, and a lysosomal and microsomal fraction were prepared by differential centrifugation. These two fractions were further centrifuged on an isopycnic Percoll gradient. The intracellularly localized form of acid phosphatase was associated with the lysosomal as well as with the microsomal fraction. In a fused rocket electrophoresis experiment these acid phosphatases cross-reacted with antiserum from seminal plasma. After neuraminidase treatment of the acid phosphatase of lysosomal and microsomal origin, only one activity band was found in polyacrylamide gels. It is concluded that only one acid phosphatase protein exists in prostatic epithelium; differences in electrophoretic mobility are caused mainly by different amounts of sialic acid residues, coupled to the same protein backbone.