Vesicles in rat epididymal fluid. Existence of two populations differing in ultrastructure and enzyme composition

FORNES WM; SOSA MA; BERTINI F; MARIO H. BURGOS

ANDROLOGIA

WILEY-BLACKWELL PUBLISHING, INC

Año: 1995 vol. 27 p. 233 - 237

0303-4569

Glycosidase activity is very high in rat epididymal fluid as a consequence of the secretory capacity  of the epithelium. The mechanism of this secretion is, so far, unknown. Membrane-bound vesicles with activity of B-galactosidase, and N-acetyl-B-D-glucosaminidase were previously  isolated by us from rat epididymal fluid. We report here the existence of two populations of epididymal vesicles separated by centrifugation in a sucrose gradient. They were found to differ in isopicnic equilibrium, size, ultrastructure and enzymatic activity. Seven days after castration the protein content and specific activity of both enzymes were found decreased in the fractions containing the vesicles. A role in enzyme secretion by the epididymal epithelium is suggested for each vesicle population.