Abstract
The ability of aliesterase, alkaline phosphatase, and acid phosphatase of mouse epididymis separated in a starch matrix by electrophoresis to attack cytochemical substrates has been investigated in tissues from normal, vasectomized, castrated, and testosterone propionate treated castrated, animals. Electrophoresis at pH 8.5 resolved 7 enzymes active against α-naphthyl propionate (designated A through G). Castration depressed the activity of A, B, and C; abolished the activity of D, E, and G; and increased the activity of F. Androgen administration restored the activity of all enzymes except that of G. D and E were more active in control animals than in vasectomized animals. Electrophoresis at pH 8.5 resolved 3 enzymes active against naphthol-AS acetate. These were identical to those designated D, E, and F above. Castration depressed the activity of D and E and increased the activity of F. Androgen treatment restored activity to levels in control animals.
Electrophoresis at pH 8.5 resolved one enzyme active against α-naphthyl phosphate at pH 8.0 (alkaline phosphatase). This enzyme was more active in tissues from vascetomized than from control animals. Castration abolished its activity and androgen treatment restored it to levels seen in control animals.
Electrophoresis at pH 8.5 resolved one enzyme active against α-naphthyl phosphate at pH 6.0 (acid phosphatase). The activity of this enzyme was similar in tissues from normal, vascetomized, castrated, and androgen treated castrated animals.