Linked Life Data

6824344

Source:http://linkedlifedata.com/resource/pubmed/id/6824344

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-3-24
pubmed:abstractText
Fatty acid synthase from the uropygial gland of goose was inhibited by treatment with pyridoxal 5'-phosphate by selectively modifying a lysine residue at the NADPH binding site of the enoyl reductase domain (A. J. Poulose and P. E. Kolattukudy (1980) Arch. Biochem. Biophys. 201, 313-321). Distribution of radioactivity in tryptic peptides generated from the synthase treated with pyridoxal 5'-phosphate/NaB3H4 in the presence and absence of 2'-monophosphoadenosine-5'-diphosphoribose, which protects the enzyme from inactivation by pyridoxal phosphate, showed that modification of one specific peptide was prevented by the protector. This peptide was purified by a combination of Sephadex G-25 column chromatography, anion-exchange chromatography, and high-performance liquid chromatography. The primary structure of this peptide is Val-Phe-Thr-Thr-Val-Gly-Ser-Ala-Glu-Lys(Pxy)-Arg.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
652-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.