Subcellular fractions were prepared from mouse kidney homogenates by differential and sucrose-gradient centrifugation. A fraction enriched in Golgi apparatus was obtained, which had considerably enriched galactosyltransferase and thiamin pyrophosphatase activities, and was morphologically typical of Golgi material. This preparation also had high β-glucuronidase activity, which increased concomitantly with microsomal β-glucuronidase activity during the specific stimulation of the enzyme in male mouse kidney after androgen administration. The degree of stimulation was much greater in the Golgi fraction. Gel-electrophoretic patterns of Golgi β-glucuronidase resembled more closely those of the enzyme located within lysosomes, but contained minor bands similar to those described previously (Swank & Paigen, 1973) as characteristic of the microsomal enzyme. It was concluded that the Golgi complex is involved in the distribution of the enzyme after its synthesis to both lysosomal and microsomal fractions.
