Linked Life Data

6267053

Source:http://linkedlifedata.com/resource/pubmed/id/6267053

Statements in which the resource exists.
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pubmed-article:6267053pubmed:abstractText[32P]ATP-citrate lyase phosphorylated by the cAMP-dependent protein kinase was partially digested by trypsin. Two tryptic 32P-labeled phosphopeptides containing more than 90% of the 32P radioactivity present on the phosphorylated enzyme were purified and found to have overlapping amino acid sequences around the same phosphorylated site (Thr-Ala-Ser(32P)-Phe-Ser-Glu-Ser-Arg). Tryptic digestion of 32P-labeled ATP-citrate lyase purified from 32P-labeled hepatocytes exposed to glucagon yielded a major 32P-labeled peptide of identical amino acid composition with that indicated above. Thus, the site on ATP-citrate lyase phosphorylated by the cAMP-dependent protein kinase in vitro resides on the same octapeptide as the site of glucagon-stimulated phosphorylation in intact hepatocytes.lld:pubmed
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pubmed-article:6267053pubmed:articleTitleATP-citrate lyase. Structure of a tryptic peptide containing the phosphorylation site directed by glucagon and the cAMP-dependent protein kinase.lld:pubmed
pubmed-article:6267053pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:6267053pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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