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Purification and properties of glycogen synthase I from bovine polymorphonuclear leucocytes |
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| Authors: | L H Rasmussen K M Pedersen H Juhl |
| Institution: | Department of Medicine and Infectious Diseases, Marselisborg Hospital, DK-8000 Aarhus C., France |
| Abstract: | 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. |
| Keywords: | purification glycogène synthase I phosphorylation leucocytes purification glycogen synthase I phosphorylation leucocytes ATP adenosine triphosphate DPCC diphenyl carbamyl chloride DTT dithiothreitol EDTA ethylendiamine tetraacetic acid Glucose-6-P glucose-6-phosphate HPLC high-performance liquid chromatography molecular ratio PMN polymorphonuclear leucocytes PMSF phenylmethylsulphonyl fluoride RI ratio of independence of glycogen synthase SDS sodium dodecyl sulphate TFA trifluoroacetic acid UDP-glucose uridine 5′-diphosphoglucose |
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