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pubmed-article:2077934pubmed:abstractTextAlkaline 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
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pubmed-article:2077934pubmed:authorpubmed-author:SiddiqiI WIWlld:pubmed
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pubmed-article:2077934pubmed:dateRevised2004-11-17lld:pubmed
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pubmed-article:2077934pubmed:articleTitleKinetic 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:2077934pubmed:affiliationInstitute Medogen S.A. 7, CH-1231 Villette, Geneva, Switzerland.lld:pubmed
pubmed-article:2077934pubmed:publicationTypeJournal Articlelld:pubmed
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