Project Details
Description
An investigation will be made of the properties and regulation of glycogen
synthase in rabbit muscle and liver in vitro and in vivo. Synthase kinases
will be purified and characterized from muscle and liver. Regulation of
kinases by calcium, calmodulin, and cyclic nucleotides will be examined.
Relationships between phosphorylation, activity, and structure of synthase
will be studied. Binding of glucose-6-P and UDP-glucose to muscle synthase
will be determined. Phosphorylation of synthase in vivo will be studied in
response to epinephrine, insulin, and diabetes. Effects of somatostatin
infusion will be examined. The in vivo phosphorylation state of each of
the sites in muscle synthase will be determined by analysis of tryptic
peptides separated by high performance liquid chromatography.
synthase in rabbit muscle and liver in vitro and in vivo. Synthase kinases
will be purified and characterized from muscle and liver. Regulation of
kinases by calcium, calmodulin, and cyclic nucleotides will be examined.
Relationships between phosphorylation, activity, and structure of synthase
will be studied. Binding of glucose-6-P and UDP-glucose to muscle synthase
will be determined. Phosphorylation of synthase in vivo will be studied in
response to epinephrine, insulin, and diabetes. Effects of somatostatin
infusion will be examined. The in vivo phosphorylation state of each of
the sites in muscle synthase will be determined by analysis of tryptic
peptides separated by high performance liquid chromatography.
| Status | Finished |
|---|---|
| Effective start/end date | 7/1/78 → 6/30/88 |
Funding
- National Institutes of Health
ASJC
- Medicine(all)
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