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Title: Translocation of uridine diphosphate N-acetylgalactosamine into vesicles derived from rat liver golgi apparatus

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6986148

N-acetylgalactosamine is the first sugar attached to the peptide backbone of many O-linked glycoproteins. A precursor in the biosynthesis of these macromolecules is UDP-GalNAc, which is synthesized in the cytosol. The mechanism by which this sugar nucleotide becomes available to the specific transferases in the lumen of the Golgi apparatus (GA) is not known. Incubation of sealed, right side out vesicles derived from rat liver GA with UDP-(/sup 3/H)GalNAc resulted in a 100-fold accumulation of soluble radioactive species within these vesicles compared to the incubation medium. Translocation of UDP-GalNAc into the lumen of GA vesicles was temperature dependent and saturable with an apparent Km of 4 ..mu..M. The specific translocation rate of UDP-GalNAc into vesicles from the GA was 5 to 10-fold higher than into vesicles derived from the rough endoplasmic reticulum (RER). The specific activity of N-acetylgalactosaminyltransferase (using apomucin as an exogenous acceptor) was 50-fold higher in membranes derived from the GA than those derived from the RER. These results strongly suggest that in rat liver the addition of GalNAc to the peptide backbone occurs in the lumen of the GA.

Research Organization:
St. Louis Univ., MO
OSTI ID:
6986148
Report Number(s):
CONF-8606151-; TRN: 86-039029
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
Country of Publication:
United States
Language:
English