Liver isozyme of glycogen synthase
Thesis/Dissertation
·
OSTI ID:5565629
The work described was aimed at comparing the liver isozymes of glycogen synthase in terms of primary structure and phosphorylation patterns, with the better studied muscle counterpart. Rat liver glycogen synthase was purified to apparent homogeneity. It was subjected to multiple phosphorylation by eight protein kinases. Phosphorylation sites were distributed between two CNBr-fragments, CB-1 (14,000) and CB-2 (28,000). Amino acid sequences of phosphopeptides of rabbit liver glycogen synthases modified by cyclic AMP-dependent protein kinase were determined and three phosphorylation sites were identified. A simple and effective procedure for determining the location of phosphorylation sites in phosphopeptides was also developed. The method employed measurement of ({sup 32}P)inorganic phosphate release during Edman degradation cycles using the gas phase sequencer. Comparison of the liver and muscle isozymes has shown that similarities are more prominent than differences and isozymes share several important properties in multiple phosphorylation and hormonal regulation.
- Research Organization:
- Indiana Univ., Bloomington, IN (USA)
- OSTI ID:
- 5565629
- Country of Publication:
- United States
- Language:
- English
Similar Records
The human liver glycogen synthase isozyme gene is located on the short arm of chromosome 12
Phosphorylation of inhibitor-2 and activation of MgATP-dependent protein phosphatase by rat skeletal muscle glycogen synthase kinase
Phosphorylation of sites 3 and 2 in rabbit skeletal muscle glycogen synthase by a multifunctional protein kinase (ATP-citrate lyase kinase)
Journal Article
·
Fri Jan 14 23:00:00 EST 1994
· Genomics; (United States)
·
OSTI ID:7077047
Phosphorylation of inhibitor-2 and activation of MgATP-dependent protein phosphatase by rat skeletal muscle glycogen synthase kinase
Conference
·
Thu May 01 00:00:00 EDT 1986
· Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
·
OSTI ID:7119682
Phosphorylation of sites 3 and 2 in rabbit skeletal muscle glycogen synthase by a multifunctional protein kinase (ATP-citrate lyase kinase)
Journal Article
·
Sat Oct 05 00:00:00 EDT 1985
· J. Biol. Chem.; (United States)
·
OSTI ID:6045590
Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CARBOHYDRATES
CHEMICAL REACTIONS
COMPARATIVE EVALUATIONS
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
ENZYMES
FRACTIONATION
GLANDS
GLYCOGEN
ISOENZYMES
ISOTOPE APPLICATIONS
ISOTOPES
LIGASES
LIGHT NUCLEI
LIVER
MAMMALS
MOLECULAR STRUCTURE
NUCLEI
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
ORGANS
PEPTIDES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
POLYSACCHARIDES
PROTEINS
RADIOISOTOPES
RATS
RODENTS
SACCHARIDES
SEPARATION PROCESSES
TRACER TECHNIQUES
TRANSFERASES
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CARBOHYDRATES
CHEMICAL REACTIONS
COMPARATIVE EVALUATIONS
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
ENZYMES
FRACTIONATION
GLANDS
GLYCOGEN
ISOENZYMES
ISOTOPE APPLICATIONS
ISOTOPES
LIGASES
LIGHT NUCLEI
LIVER
MAMMALS
MOLECULAR STRUCTURE
NUCLEI
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
ORGANS
PEPTIDES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
POLYSACCHARIDES
PROTEINS
RADIOISOTOPES
RATS
RODENTS
SACCHARIDES
SEPARATION PROCESSES
TRACER TECHNIQUES
TRANSFERASES
VERTEBRATES