Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1983-1-7
pubmed:abstractText
The fate of UDP formed during the galactosylation of added N-acetylglucosamine in Golgi vesicles isolated from rat liver using D2O-sucrose gradients has been determined. UDP-Gal labeled with [14C]uracil was used, and the products of the reaction were separated and quantitated by using high-pressure liquid chromatography. [14C]Uridine rather than [14C]UDP or [14C]UMP was found to accumulate, indicating the presence of both UDPase and UMPase activities in the Golgi. Golgi vesicles were shown to contain a nucleosidediphosphatase activity that is membrane bound. It appears to be located on the luminal face of the Golgi since it is activated 3-5-fold by detergents and 4-fold by treatment of the vesicles with Filipin. We have shown previously that Filipin disrupts the Golgi but does not solubilize membrane-bound enzymes. The nucleosidediphosphatase of the Golgi differs from that present in rough endoplasmic reticulum in its absolute requirement for Ca2+ for activity and in its substrate specificity that is higher for UDP than for IDP. Golgi vesicles also contain UMPase activity that is stimulated only 2-fold by detergents or Filipin. Concanavalin A inhibits this activity about 80% in both intact and detergent-treated vesicles. The Golgi UMPase is thus probably identical with 5'-nucleotidase. These results are consistent with histochemical evidence from other laboratories that indicate that 5'-nucleotidase is present on both sides of liver Golgi membranes. In the presence of concanavalin A and N-acetylglucosamine, intact Golgi vesicles were found to convert UDP-Gal to UMP. These findings indicate that UDP formed by galactosyltransferase in the lumen of the vesicles is rapidly converted to UMP by UDPase in the lumen but that UMP moves rapidly out of the lumen of the Golgi and is broken down to uridine by 5'-nucleotidase on the cytoplasmic side of the vesicles.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4640-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Orientation and role of nucleosidediphosphatase and 5'-nucleotidase in Golgi vesicles from rat liver.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.