Insulin receptor was examined as a substrate for the multipotential protein kinase casein kinase I. Casein kinase I phosphorylated partially purified insulin receptor from human placenta as shown by immunoprecipitation of the complex with antiserum to the insulin receptor. Analysis of the phosphoryl
Inhibition of insulin receptor phosphorylation by indomethacin
β Scribed by Carl D. Malchoff; Joseph L. Messina; Valery Gordon; Shinri Tamura; Joseph Larner
- Publisher
- Springer
- Year
- 1985
- Tongue
- English
- Weight
- 702 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0300-8177
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Purified postsynaptic membranes can be used as a model system to study the regulation of synaptic membrane proteins. These membranes contain protein kinase activity that phosphorylates the acetylcholine receptor (AChR). We find that diphenylhydantoin (DPH) interacts with these membranes
Various glycolytic and gluconeogenic enzymes were tested as substrates for the insulin receptor kinase. Phosphofructokinase and phosphoglycerate mutase were found to be the best substrates. Phosphorylation of these enzymes was rapid, stimulated 2-to 6-fold by M insulin and occurred exclusively on ty
The rapid phase of fructose-l,6-bisphosphatase (FBPase) inactivation following glucose addition to starved yeast cells [reported previously] is inhibited on addition of 10 mM chloroquine (CQ) at about pH 8. This inhibition of inactivation was shown to be due to the prevention of phosphorylation of t