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  Annali italiani di chirurgia

  Digital Access Ann Ital Chir v. 71-, 2000-

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  v. 1, 6, 15, [16-17, 23, 25-27], 30-48, [49], 1922, 1927, 1936, [1937-38, 1946, 1948-50], 1953-74, [1975].

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  Multiple phosphorylation of acetyl-CoA carboxylase in chick liver cells. A cyclic AMP-independent process.

  Pekala PH, Meredith MJ, Tarlow DM, Lane MD.

  J Biol Chem. 1978 Aug 10;253(15):5267-9.

  When chick liver cells in monolayer culture were incubated with 32Pi in the presence of insulin, acetyl-CoA carboxylase became extensively labeled with 32Pi reaching a stoichiometry of 9 to 10 mol of phosphoryl group per mol of 240,000-dalton enzyme subunit. The covalently bound phosphate was found to be metabolically labile, turning over with a t1/2 of approximately 2 h (enzyme t1/2 approximately equal to 24 h). Addition of Bt2cAMP altered neither the rate nor extent of phosphorylation. Contrary to other reports, the fully phosphorylated acetyl-CoA carboxylase appears to be catalytically active.

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