Isolation of a Golgi rich fraction from rat ventral prostate.
Unmodified procedures for isolation of fractions rich in Golgi elements from other tissues have not proved applicable to the rat ventral prostate because of the tendency of membranous material to aggregate. We have devised a new procedure whereby: 1) a Golgi rich fraction from rat ventral prostate was released by a gentle two-step homogenization and isolated by centrifugation through discontinuous sucrose density gradients; 2) the specific activity of UDP-galactose: glycoprotein galactosyltransferase increased 69-fold in this fraction; 3) the isolated Golgi fraction was reasonably free from mitochondria, lysosomes, endoplasmic reticulum and plasma membranes as shown by the relatively low activities of marker enzymes; 4) the specific activities of acid phosphatase and 5'-nucleotidase in the Golgi rich fraction was 4 times greater than that in prostate homogenate. Both enzymes are secretory products and their presence in Golgi elements is probably associated with their packaging in secretory granules.
D015720:5'-Nucleotidase; D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D006056:Golgi Apparatus / Q000648:ultrastructure*; D008297:Male; D009708:Nucleotidases / Q000378:metabolism; D011467:Prostate / Q000648:ultrastructure*; D051381:Rats; D006022:beta-N-Acetylglucosaminylglycopeptide beta-1,4-Galactosyltransferase / Q000378:metabolism
D006022:beta-N-Acetylglucosaminylglycopeptide beta-1,4-Galactosyltransferase; D009708:Nucleotidases; D000135:Acid Phosphatase; D015720:5'-Nucleotidase