pubmed-article:3107615 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3107615 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:3107615 | lifeskim:mentions | umls-concept:C0596040 | lld:lifeskim |
pubmed-article:3107615 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3107615 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
pubmed-article:3107615 | lifeskim:mentions | umls-concept:C1516893 | lld:lifeskim |
pubmed-article:3107615 | lifeskim:mentions | umls-concept:C0204514 | lld:lifeskim |
pubmed-article:3107615 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:3107615 | pubmed:dateCreated | 1987-7-15 | lld:pubmed |
pubmed-article:3107615 | pubmed:abstractText | The interaction of benzamide with the isolated components of calf thymus poly(ADP-ribose) polymerase and with liver nuclei has been investigated. A benzamide-agarose affinity gel matrix was prepared by coupling o-aminobenzoic acid with Affi-Gel 10, followed by amidation. The benzamide-agarose matrix bound the DNA that is coenzymic with poly(ADP-ribose) polymerase; the matrix, however, did not bind the purified poly(ADP-ribose) polymerase protein. A highly radioactive derivative of benzamide, the 125I-labelled adduct of o-aminobenzamide and the Bolton-Hunter reagent, was prepared and its binding to liver nuclear DNA, calf thymus DNA and specific coenzymic DNA of poly(ADP-ribose) polymerase was compared. The binding of labelled benzamide to coenzymic DNA was several-fold higher than its binding to unfractionated calf thymus DNA. A DNA-related enzyme inhibitory site of benzamide was demonstrated in a reconstructed poly(ADP-ribose) polymerase system, made up from purified enzyme protein and varying concentrations of a synthetic octadeoxynucleotide that serves as coenzyme. As a model for benzamide binding to DNA, a crystalline complex of 9-ethyladenine and benzamide was prepared and its X-ray crystallographic structure was determined; this indicated a specific hydrogen bond between an amide hydrogen atom and N-3 of adenine. The benzamide also formed a hydrogen bond to another benzamide molecule. The aromatic ring of benzamide does not intercalate between ethyladenine molecules, but lies nearly perpendicular to the planes of stacking ethyladenine molecules in a manner reminiscent of the binding of ethidium bromide to polynucleotides. Thus we have identified DNA as a site of binding of benzamide; this binding is critically dependent on the nature of the DNA and is high for coenzymic DNA that is isolated with the purified enzyme as a tightly associated species. A possible model for such binding has been suggested from the structural analysis of a benzamide-ethyladenine complex. | lld:pubmed |
pubmed-article:3107615 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:language | eng | lld:pubmed |
pubmed-article:3107615 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3107615 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3107615 | pubmed:month | Jun | lld:pubmed |
pubmed-article:3107615 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:3107615 | pubmed:author | pubmed-author:KunEE | lld:pubmed |
pubmed-article:3107615 | pubmed:author | pubmed-author:BauerP IPI | lld:pubmed |
pubmed-article:3107615 | pubmed:author | pubmed-author:HakamAA | lld:pubmed |
pubmed-article:3107615 | pubmed:author | pubmed-author:GluskerJ PJP | lld:pubmed |
pubmed-article:3107615 | pubmed:author | pubmed-author:ZachariasD... | lld:pubmed |
pubmed-article:3107615 | pubmed:author | pubmed-author:McLickJJ | lld:pubmed |
pubmed-article:3107615 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3107615 | pubmed:day | 6 | lld:pubmed |
pubmed-article:3107615 | pubmed:volume | 909 | lld:pubmed |
pubmed-article:3107615 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3107615 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3107615 | pubmed:pagination | 71-83 | lld:pubmed |
pubmed-article:3107615 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:meshHeading | pubmed-meshheading:3107615-... | lld:pubmed |
pubmed-article:3107615 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3107615 | pubmed:articleTitle | Benzamide-DNA interactions: deductions from binding, enzyme kinetics and from X-ray structural analysis of a 9-ethyladenine-benzamide adduct. | lld:pubmed |
pubmed-article:3107615 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3107615 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3107615 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:3107615 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |