pubmed-article:2077934 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C0016327 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C1149888 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C0206189 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C1705938 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:2077934 | lifeskim:mentions | umls-concept:C0128922 | lld:lifeskim |
pubmed-article:2077934 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2077934 | pubmed:dateCreated | 1991-4-25 | lld:pubmed |
pubmed-article:2077934 | pubmed:abstractText | Alkaline phosphatase catalyzes the hydrolytic cleavage of the P-F bond in monofluorophosphate with the subsequent release of fluoride ions. A kinetic potentiometric method is described in which a fluoride ion-selective electrode is used for the sensitive and selective measurement of the released F- for the determination of alkaline phosphatase activity. It is shown that monofluorophosphate can be used as an alternative substrate for alkaline phosphatase. The reaction demonstrates a well-defined correlation with the hydrolysis of the P-O bond in 4-nitrophenyl phosphate. The serum alkaline phosphatase was determined in human serum samples by the potentiometric technique, and the results obtained compared well with a standard spectrophotometric method. | lld:pubmed |
pubmed-article:2077934 | pubmed:language | eng | lld:pubmed |
pubmed-article:2077934 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2077934 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2077934 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2077934 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2077934 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2077934 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2077934 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2077934 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2077934 | pubmed:issn | 0003-2697 | lld:pubmed |
pubmed-article:2077934 | pubmed:author | pubmed-author:ManganCC | lld:pubmed |
pubmed-article:2077934 | pubmed:author | pubmed-author:SiddiqiI WIW | lld:pubmed |
pubmed-article:2077934 | pubmed:author | pubmed-author:VenetzW PWP | lld:pubmed |
pubmed-article:2077934 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2077934 | pubmed:day | 15 | lld:pubmed |
pubmed-article:2077934 | pubmed:volume | 191 | lld:pubmed |
pubmed-article:2077934 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2077934 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2077934 | pubmed:pagination | 127-32 | lld:pubmed |
pubmed-article:2077934 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:meshHeading | pubmed-meshheading:2077934-... | lld:pubmed |
pubmed-article:2077934 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2077934 | pubmed:articleTitle | Kinetic determination of alkaline phosphatase activity based on hydrolytic cleavage of the P-F bond in monofluorophosphate and fluoride ion-selective electrode. | lld:pubmed |
pubmed-article:2077934 | pubmed:affiliation | Institute Medogen S.A. 7, CH-1231 Villette, Geneva, Switzerland. | lld:pubmed |
pubmed-article:2077934 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2077934 | lld:pubmed |