Lysosomal enzymes in cells separated from rat testis

Fractions enriched with Sertoli cell (S), germ cells (G), and interstitial cells (I) were separated from rat testis after enzymic treatment and double filtration through nylon meshes. The fractions were analysed for protein content and for enzymic activity of 4 acid hydrolases known to be of lysosomal nature in other tissues. Acid phosphatase activity was preferentially recovered in Fraction G, the highest activity of beta-glucuronidase was found in Fraction I while the activity of aryl sulphatase and beta-N-acetyl-D-glucosaminidase was prominent in Fraction S. With the exception of acid phosphatase, the enzymes were mostly recovered in a subcellular fraction of whole testis homogenate separated between 600 and 27 000 g. The results may reflect the peculiar enzyme composition of the lysosomal apparatus of each cell type.