Purification and properties of glycogen synthase I from bovine polymorphonuclear leucocytes.
Glycogen synthase I was purified from bovine polymorphonuclear leucocytes (PMNs) by a procedure involving concanavalin A-Sepharose affinity chromatography. The purified glycogen-bound glycogen synthase I had a specific activity of 9.83 U/mg protein and the glycogen free enzyme 21 U/mg protein. Molecular ratio of the native enzyme and the subunit were 340 K and 85 K respectively. After phosphorylation by the catalytic subunit of cAMP-dependent protein kinase the phosphorylated sites were studied using high-performance liquid chromatography (HPLC) of the tryptic 32P-peptides. The enzyme was phosphorylated at three different sites with retention times identical to site 1a, site 1b, and site 2 from rabbit skeletal muscle glycogen synthase.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D000242:Cyclic AMP / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006006:Glycogen Synthase / Q000097:blood*; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology*; D010446:Peptide Fragments / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D000516:alpha-Amylases / Q000378:metabolism
D010446:Peptide Fragments; D000242:Cyclic AMP; D006006:Glycogen Synthase; D011494:Protein Kinases; D000516:alpha-Amylases; D014357:Trypsin