Phosphorylation of sites 3 and 4 in rabbit skeletal muscle glycogen synthase by cAMP-dependent protein kinase.
作者： V S Sheorain , J D Corbin , T R Soderling
DOI: 10.1016/S0021-9258(18)89631-4
关键词:
摘要: Rabbit skeletal muscle glycogen synthase (synthase a) can be phosphorylated by 0.2 to 2.5 microM catalytic subunit of cAMP-dependent protein kinase a stoichiometry 1.5 3 mol 32PO4/subunit (90,000 X g). When complete tryptic digest this 32P-synthase was chromatographed on reverse phase high performance liquid chromatography, it observed that, in addition sites 1a, 1b, and 2, site phosphorylated. The peptide containing 5 also contained 32PO4, but sequence analysis identified new phosphorylation site, 4 (Arg-His-Ser-Ser(PO4)-) which precedes 5. Phosphorylation became significant when the total exceeded mol/subunit. heat-stable inhibitor or regulatory decreased all sites, including 4. holoenzyme form highly dependent presence cAMP. These results establish that these is due itself not contaminating kinase(s). Synthase b from control rabbit muscle, 2 phosphate/subunit, incorporated up 2.0 32PO4 catalyzed vitro kinase. Again, detected as well 2. suggest vivo after injection epinephrine rabbits could solely known activation
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