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rdf:type |
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lifeskim:mentions |
umls-concept:C0007452,
umls-concept:C0018787,
umls-concept:C0034344,
umls-concept:C0205145,
umls-concept:C0205225,
umls-concept:C0449432,
umls-concept:C0678594,
umls-concept:C1179435,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248
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pubmed:issue |
3
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pubmed:dateCreated |
1987-11-18
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pubmed:abstractText |
Bovine heart pyruvate dehydrogenase complex was acetylated by using [3-14C]pyruvate in the presence of N-ethylmaleimide, with approx. 1 mol of acetyl groups being incorporated per mol of E2 polypeptide. After peptic digestion, lipoate-containing peptides were purified by high-voltage electrophoresis and ion-exchange and reverse-phase h.p.l.c. The amino acid sequence around the lipoic acid-attachment site of E2 was determined by automated Edman degradation. Acetylation of a lipoate cofactor bound to a lysine residue was verified by fast-atom-bombardment m.s.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-200908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-3089786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-3101735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-3522581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-371616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-3944115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-4006943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-4401694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-6345153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-6376124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-6770865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-6778866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-6801041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-6821375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-7286238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-7470091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-762164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3117054-795424
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
245
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
919-22
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3117054-Acetylation,
pubmed-meshheading:3117054-Amino Acid Sequence,
pubmed-meshheading:3117054-Animals,
pubmed-meshheading:3117054-Cattle,
pubmed-meshheading:3117054-Ethylmaleimide,
pubmed-meshheading:3117054-Mass Spectrometry,
pubmed-meshheading:3117054-Molecular Sequence Data,
pubmed-meshheading:3117054-Myocardium,
pubmed-meshheading:3117054-Peptide Fragments,
pubmed-meshheading:3117054-Pyruvate Dehydrogenase (Lipoamide),
pubmed-meshheading:3117054-Pyruvate Dehydrogenase Complex,
pubmed-meshheading:3117054-Pyruvates,
pubmed-meshheading:3117054-Pyruvic Acid,
pubmed-meshheading:3117054-Thioctic Acid
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pubmed:year |
1987
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pubmed:articleTitle |
Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex.
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pubmed:affiliation |
Department of Biochemistry, University of Newcastle upon Tyne, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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