rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
17
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pubmed:dateCreated |
1981-10-29
|
pubmed: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.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
256
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
8867-70
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:6267053-ATP Citrate (pro-S)-Lyase,
pubmed-meshheading:6267053-Amino Acid Sequence,
pubmed-meshheading:6267053-Amino Acids,
pubmed-meshheading:6267053-Animals,
pubmed-meshheading:6267053-Cyclic AMP,
pubmed-meshheading:6267053-Glucagon,
pubmed-meshheading:6267053-Liver,
pubmed-meshheading:6267053-Macromolecular Substances,
pubmed-meshheading:6267053-Male,
pubmed-meshheading:6267053-Peptide Fragments,
pubmed-meshheading:6267053-Phosphorylation,
pubmed-meshheading:6267053-Protein Kinases,
pubmed-meshheading:6267053-Rats,
pubmed-meshheading:6267053-Rats, Inbred Strains,
pubmed-meshheading:6267053-Trypsin
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pubmed:year |
1981
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pubmed:articleTitle |
ATP-citrate lyase. Structure of a tryptic peptide containing the phosphorylation site directed by glucagon and the cAMP-dependent protein kinase.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|