pubmed-article:3663623 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0016411 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0025677 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0039667 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C1548779 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C1947902 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C2827499 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
pubmed-article:3663623 | lifeskim:mentions | umls-concept:C1167624 | lld:lifeskim |
pubmed-article:3663623 | pubmed:issue | 15 | lld:pubmed |
pubmed-article:3663623 | pubmed:dateCreated | 1987-12-7 | lld:pubmed |
pubmed-article:3663623 | pubmed:abstractText | N alpha-(4-Amino-4-deoxy-10-methylpteroyl)-N epsilon-(4-azido-5- [125I]iodosalicylyl)-L-lysine, a photoaffinity analogue of methotrexate, is only 2-fold less potent than methotrexate in the inhibition of murine L1210 dihydrofolate reductase. Irradiation of the enzyme in the presence of an equimolar concentration of the 125I-labeled analogue ultimately leads to an 8% incorporation of the photoprobe. A 100-fold molar excess of methotrexate essentially blocks this incorporation. Cyanogen bromide digestion of the labeled enzyme, followed by high-pressure liquid chromatography purification of the generated peptides, indicates that greater than 85% of the total radioactivity is incorporated into a single cyanogen bromide peptide. Sequence analysis revealed this peptide to be residues 53-111, with a majority of the radioactivity centered around residues 63-65 (Lys-Asn-Arg). These data demonstrate that the photoaffinity analogue specifically binds to dihydrofolate reductase and covalently modifies the enzyme following irradiation and is therefore a photolabeling agent useful for probing the inhibitor binding domain of the enzyme. | lld:pubmed |
pubmed-article:3663623 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:language | eng | lld:pubmed |
pubmed-article:3663623 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3663623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3663623 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3663623 | pubmed:month | Jul | lld:pubmed |
pubmed-article:3663623 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:3663623 | pubmed:author | pubmed-author:SmithP LPL | lld:pubmed |
pubmed-article:3663623 | pubmed:author | pubmed-author:FreisheimJ... | lld:pubmed |
pubmed-article:3663623 | pubmed:author | pubmed-author:PriceE MEM | lld:pubmed |
pubmed-article:3663623 | pubmed:author | pubmed-author:KleinT ETE | lld:pubmed |
pubmed-article:3663623 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3663623 | pubmed:day | 28 | lld:pubmed |
pubmed-article:3663623 | pubmed:volume | 26 | lld:pubmed |
pubmed-article:3663623 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3663623 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3663623 | pubmed:pagination | 4751-6 | lld:pubmed |
pubmed-article:3663623 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:3663623 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3663623 | pubmed:articleTitle | Photoaffinity analogues of methotrexate as folate antagonist binding probes. 1. Photoaffinity labeling of murine L1210 dihydrofolate reductase and amino acid sequence of the binding region. | lld:pubmed |
pubmed-article:3663623 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Cincinnati College of Medicine, Ohio 45267-0522. | lld:pubmed |
pubmed-article:3663623 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3663623 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3663623 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |