Amino-terminal sequence analysis of rat heart and muscle glycogen synthase: homology to the rabbit enzyme and the implications for hormonal control.
Glycogen synthase was purified from rat heart and muscle and electroblotted from sodium dodecyl sulfate polyacrylamide gels to polyvinylidene difluoride, and the NH2-terminal amino acid sequence was determined. The NH2-terminal amino acid sequence of the enzymes was identical. Further, phosphorylation site 2, a major cyclic AMP-dependent protein kinase recognition site in the rabbit muscle isozyme, is conserved in the rat isozymes suggesting that it serves an important function in hormonal regulation. However, two potentially important differences were observed. Threonine-5 and valine-8 of the rabbit muscle enzyme are serine and methionine residues, respectively, in the rat isozyme, the latter being critical in the analysis of phosphopeptides produced by cyanogen bromide cleavage. These variations may provide a partial explanation for previously observed differences in rat and rabbit phosphopeptide maps.
Jaspers
S R
SR
Department of Biochemistry, University of Massachusetts Medical Center, Worcester 01605.
Rulfs
J
J
Johnson
G L
GL
Mole
J E
JE
Miller
T B
TB
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D006006:Glycogen Synthase / Q000302:isolation & purification; D009132:Muscles / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D006006:Glycogen Synthase