Key points are not available for this paper at this time.
Abstract A procedure has been developed for the isolation of morphologically recognizable, largely intact, Golgi apparatus from rat kidneys. The fraction contains both uridine diphosphogalactose: N-acetylglucosamine galactosyltransferase and 3'-phosphoadenosine 5'-phosphosulfate: cerebroside sulfotransferase activities enriched 50- to 80-fold over the original homogenate. Comparison of the Golgi-rich fraction with plasma membranes, endoplasmic reticulum, mitochondria, and nuclei isolated from rat kidney indicates that the Golgi apparatus is the main locus of both of these enzymes in kidney cells. Golgi apparatus from rat liver, although rich in galactosyltransferase, appears to be devoid of the sulfotransferase. The cerebroside sulfotransferase of kidney Golgi forms sulfatide from added galactocerebrosides. Both hydroxyfatty acid and normal fatty acid-containing cerebrosides are sulfated. The enzyme is activated almost maximally by the addition of as little as 0.1% Triton X-100. The presence of 60 mm Mn2+ stimulates the activity about 3-fold. The apparent Km for cerebrosides was 1.3 x 10-4, m, while that for 3'-phosphoadenosine 5'-phosphosulfate was 2.1 x 10-3 m. These results show that the Golgi apparatus in kidney cells can function to modify glycolipids as well as glycoproteins.
Fleischer et al. (1974) studied this question.