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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
|
pubmed:dateCreated |
1988-4-5
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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)).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorus Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Poly Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/poly ADP-ribose glycohydrolase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0829-8211
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
668-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3325077-Animals,
pubmed-meshheading:3325077-Cattle,
pubmed-meshheading:3325077-Cell Nucleus,
pubmed-meshheading:3325077-Glycoside Hydrolases,
pubmed-meshheading:3325077-Phosphorus Radioisotopes,
pubmed-meshheading:3325077-Poly Adenosine Diphosphate Ribose,
pubmed-meshheading:3325077-Radioisotope Dilution Technique,
pubmed-meshheading:3325077-Thymus Gland
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pubmed:year |
1987
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pubmed:articleTitle |
Rapid assay of poly(ADP-ribose) glycohydrolase.
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pubmed:affiliation |
Département de Biologie, Faculté des Sciences, Université de Sherbrooke, Qué., Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|