Document Detail


Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney 2-oxoglutarate dehydrogenase complex.
MedLine Citation:
PMID:  3115829     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The 2-oxoglutarate dehydrogenase complex was succinylated using 2-oxo[5-14C]glutarate in the presence of N-ethylmaleimide to label the lipoic acid cofactor of the transuccinylase (E2) component. Following peptic digestion, 14C-lipoate-containing peptides were purified and subjected to automated Edman degradation and amino acid analysis. The amino acid sequence surrounding the lipoyllysine residue is reported.
Authors:
A P Bradford; A Aitken; F Beg; K G Cook; S J Yeaman
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  222     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1987 Sep 
Date Detail:
Created Date:  1987-11-12     Completed Date:  1987-11-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  211-4     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Newcastle upon Tyne, England.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Carbon Radioisotopes
Cattle
Ketoglutarate Dehydrogenase Complex / metabolism*
Ketoglutaric Acids / metabolism
Ketone Oxidoreductases / metabolism*
Kidney Cortex / enzymology*
Peptide Fragments / analysis
Thioctic Acid*
Chemical
Reg. No./Substance:
0/Carbon Radioisotopes; 0/Ketoglutaric Acids; 0/Peptide Fragments; 328-50-7/alpha-ketoglutaric acid; 62-46-4/Thioctic Acid; EC 1.2.-/Ketone Oxidoreductases; EC 1.2.4.2/Ketoglutarate Dehydrogenase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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