| pubmed-article:3325077 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3325077 | lifeskim:mentions | umls-concept:C0071349 | lld:lifeskim |
| pubmed-article:3325077 | lifeskim:mentions | umls-concept:C1418269 | lld:lifeskim |
| pubmed-article:3325077 | lifeskim:mentions | umls-concept:C1510438 | lld:lifeskim |
| pubmed-article:3325077 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:3325077 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:3325077 | pubmed:dateCreated | 1988-4-5 | lld:pubmed |
| pubmed-article:3325077 | pubmed:abstractText | We have developed a rapid, highly reproducible assay to determine poly(ADP-ribose) glycohydrolase activity which measures directly the appearance of the reaction product. We also analysed the majority of different techniques which are used to determine poly(ADP-ribose) glycohydrolase activity and found that the apparent activity can vary extensively depending on the method used. Thin-layer chromatography using PEI-F-cellulose was the only method which evaluated directly the specific release of ADP-ribose; by comparison with this method, the other procedures gave an over- or under-estimation of 2- to 10-fold of the enzymatic activity. A rapid method of affinity chromatography has also been developed to synthesize and purify in high yield poly(ADP-ribose) (35% conversion of 1 mM NAD to poly(ADP-ribose)). | lld:pubmed |
| pubmed-article:3325077 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3325077 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3325077 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3325077 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3325077 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:3325077 | pubmed:issn | 0829-8211 | lld:pubmed |
| pubmed-article:3325077 | pubmed:author | pubmed-author:PoirierG GGG | lld:pubmed |
| pubmed-article:3325077 | pubmed:author | pubmed-author:MénardLL | lld:pubmed |
| pubmed-article:3325077 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3325077 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:3325077 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3325077 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3325077 | pubmed:pagination | 668-73 | lld:pubmed |
| pubmed-article:3325077 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3325077 | pubmed:meshHeading | pubmed-meshheading:3325077-... | lld:pubmed |
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| pubmed-article:3325077 | pubmed:meshHeading | pubmed-meshheading:3325077-... | lld:pubmed |
| pubmed-article:3325077 | pubmed:meshHeading | pubmed-meshheading:3325077-... | lld:pubmed |
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| pubmed-article:3325077 | pubmed:meshHeading | pubmed-meshheading:3325077-... | lld:pubmed |
| pubmed-article:3325077 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3325077 | pubmed:articleTitle | Rapid assay of poly(ADP-ribose) glycohydrolase. | lld:pubmed |
| pubmed-article:3325077 | pubmed:affiliation | Département de Biologie, Faculté des Sciences, Université de Sherbrooke, Qué., Canada. | lld:pubmed |
| pubmed-article:3325077 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3325077 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:3325077 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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