phosphorus-radioisotopes has been researched along with glucose-1-phosphate* in 2 studies
2 other study(ies) available for phosphorus-radioisotopes and glucose-1-phosphate
| Article | Year |
|---|---|
Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver.
Parafusin, the major protein in Paramecium tetraurelia to undergo dephosphorylation in response to secretory stimuli, appears to be the primary acceptor for the glucosylphosphotransferase in this species based on five independent criteria: identical molecular size of 63 kD; identical isoelectric points in the phosphorylated state of pH 5.8 and 6.2; identical behavior in reverse-phase chromatography; immunological cross-reactivity with an affinity-purified anti-parafusin antibody; the presence of a phosphorylated sugar after acid hydrolysis. It appears likely that the dephosphorylation observed with secretion reflects the removal of alpha Glc-1-P from parafusin's oligosaccharides and is consistent, therefore, with a regulatory role for this cytoplasmic glycosylation event. The glucosylphosphotransferase acceptor in rat liver is also immunoprecipitated by the anti-parafusin antibody and is very similar in physical characteristics to the paramecium protein. This conservation suggests a role for parafusin in mammalian exocytosis as well, at a step common to both the regulated and constitutive secretory pathways. Topics: Animals; Glucosephosphates; Glycosylation; Hydrolysis; In Vitro Techniques; Liver; Mannose; Molecular Weight; Paramecium; Phosphoproteins; Phosphorus Radioisotopes; Phosphorylation; Phosphotransferases; Precipitin Tests; Rats; Substrate Specificity; Transferases (Other Substituted Phosphate Groups) | 1990 |
The beta-phosphoro[35S]thioate analogue of UDP-Glc is efficiently utilized by the glucose phosphotransferase and is relatively resistant to hydrolytic degradation.
The beta-phosphoro[35S]thioate analogue of UDP-glucose ((beta-35S)UDP-Glc) is utilized with approximately the same efficiency as the parent compound by the UDP-glucose:glycoprotein glucose-1-phosphotransferase (glucosyltransferase), which catalyzes the transfer of alpha Glc-1-P from UDP-Glc to mannose-containing oligosaccharides on acceptor glycoproteins. The same endogenous acceptor glycoproteins are labeled by the glucosyltransferase using [beta-32P]UDP-Glc and (beta-35S)UDP-Glc. However, in liver homogenates, incorporation from [beta-32P]UDP-Glc ceases to increase after about 4 min of incubation, while incorporation from (beta-35S)UDP-Glc persists for at least 1 h. This difference is due to an approx. 10-fold slower hydrolytic rate for the phosphorothioate analogue than for the parent compound, a finding similar to previous work showing that a variety of nucleases and phosphodiesterases are less efficient in cleaving phosphorothioate DNA than the native polymer. Topics: Animals; Chick Embryo; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Glucosephosphates; Hydrolysis; Kinetics; Liver; Male; Molecular Weight; Phosphorus Radioisotopes; Phosphotransferases; Rats; Rats, Inbred Strains; Sulfur Radioisotopes; Transferases (Other Substituted Phosphate Groups); Uridine Diphosphate Glucose; Uridine Diphosphate Sugars | 1987 |