Kinetic determination of alkaline phosphatase activity based on hydrolytic cleavage of the P-F bond in monofluorophosphate and fluoride ion-selective electrode.
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.
Venetz
W P
WP
Institute Medogen S.A. 7, CH-1231 Villette, Geneva, Switzerland.
Mangan
C
C
Siddiqi
I W
IW
D000469:Alkaline Phosphatase / Q000097:blood*; D004566:Electrodes; D005459:Fluorides / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010710:Phosphates / Q000737:chemistry / Q000378:metabolism*
D010710:Phosphates; C012980:fluorophosphate; D000469:Alkaline Phosphatase; D005459:Fluorides