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- W1998021240 abstract "This study reports a partial characterization of a 15,000 dalton (15 kDa) proteolipid present in rat skeletal muscle sarcolemma. The proteolipid is phosphorylated by both cyclic AMP-dependent and calcium/phospholipid-dependent protein kinases, displays an isoelectric point (pI) of 5.9, and can be extracted from sarcolemma by acidified chloroform/methanol (2:1) or non-ionic detergents. Phosphoamino acid analysis and tryptic fingerprinting of the phosphorylated proteolipid indicate that both cyclic AMP- and calcium/phospholipid-dependent protein kinases predominantly phosphorylate serine residue(s) on a single tryptic peptide. Additivity experiments and thermolytic fingerprinting demonstrate a minimum of two distinct phosphorylation sites on the proteolipid, the phosphorylation of which is independently catalyzed by cyclic AMP-dependent and calcium/phospholipid-dependent protein kinases in vitro. This sarcolemma proteolipid, which appears to be identified to a sarcolemma protein previously reported to be phosphorylated upon addition of insulin in a GTP-dependent manner (Walaas, O., Walaas, E., Rye-Alertsen, A. and Horn, R.S. (1979) Mol. Cell. Endocrinol. 16, 45-55), therefore represents a possible membrane target for those neuronal and hormonal stimuli which can regulate cyclic AMP-dependent or calcium/phospholipid-dependent protein kinase activities in skeletal muscle." @default.
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- W1998021240 date "1988-01-01" @default.
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- W1998021240 title "Phosphorylation of multiple sites in a 15 000 dalton proteolipid from rat skeletal muscle sarcolemma, catalyzed by adenosine 3′,5′-monophosphate-dependent and calcium / phospholipid-dependent protein kinases" @default.
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- W1998021240 doi "https://doi.org/10.1016/0167-4889(88)90052-3" @default.
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