| pubmed-article:6279 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6279 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:6279 | lifeskim:mentions | umls-concept:C0012476 | lld:lifeskim |
| pubmed-article:6279 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6279 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:6279 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6279 | pubmed:dateCreated | 1976-9-2 | lld:pubmed |
| pubmed-article:6279 | pubmed:abstractText | NAD glycohydrolase of calf spleen was solubilized with pancreatic lipase and purified approximatively 800-fold to a specific activity of 7 units/mg of protein by successive DEAE-cellulose and carboxymethyl-cellulose chromatography. The purified enzyme has a molecular weight of 24,000 and is characterized by a double band on disc gel electrophoresis. Some kinetic properties of the NAD-glycohydrolase-catalyzed hydrolsis of NAD have been examined using a titrimetric assay for enzyme activity. The reaction is subject to inhibition be excess of substrate, which disappears at high ionic strength and low pH. At a pH below 5 the kinetic displays an apparent activation by substrate. The effects of pH (4.5-9.0) on the kinetic parameters do not reveal an essential ionizable group in the catalytic process. | lld:pubmed |
| pubmed-article:6279 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6279 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6279 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6279 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6279 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6279 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6279 | pubmed:month | May | lld:pubmed |
| pubmed-article:6279 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:6279 | pubmed:author | pubmed-author:SchuberFF | lld:pubmed |
| pubmed-article:6279 | pubmed:author | pubmed-author:TravoPP | lld:pubmed |
| pubmed-article:6279 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6279 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:6279 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:6279 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6279 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6279 | pubmed:pagination | 247-55 | lld:pubmed |
| pubmed-article:6279 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Ani... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Spl... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Hyd... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Cat... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Kin... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-NAD | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-N-G... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Osm... | lld:pubmed |
| pubmed-article:6279 | pubmed:meshHeading | pubmed-meshheading:6279-Sol... | lld:pubmed |
| pubmed-article:6279 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:6279 | pubmed:articleTitle | Calf-spleen nicotinamide--adenine dinucleotide glycohydrolase. Solubilization purification and properties of the enzyme. | lld:pubmed |
| pubmed-article:6279 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6279 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6279 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6279 | lld:pubmed |
