Amplified luminometric assays of alkaline phosphatase using riboflavin phosphates
- 1 October 1991
- journal article
- research article
- Published by Wiley in Journal of Bioluminescence and Chemiluminescence
- Vol. 6 (4) , 251-258
- https://doi.org/10.1002/bio.1170060407
Abstract
An asasy for alkaline phosphatase is described which is based on the hydrolysis of riboflavin phosphates (5′FMN or 4′FMN) to produce riboflavin. This is converted to 5′FMN using riboflavin kinase, and then asayed using the bacterial bioluminescent system from Vibrio harveyi or V. Fischeri. The most sensitive assay is obtained using 4′FMN, which can measure less than 20 amol after a 1-hour incubation.Keywords
This publication has 6 references indexed in Scilit:
- A comparison of chemiluminescent and colorimetric substrates in a hepatitis B virus DNA hybridization assayAnalytical Biochemistry, 1989
- Preparation of oligodeoxynucleotide-alkaline phosphatase conjugates and their use hybridization probesNucleic Acids Research, 1986
- Plant flavokinase. Affinity-chromatographic procedure for the purification of the enzyme from mung-bean (Phaseolus aureus) seeds and conformational changes on its interaction with orthophosphateBiochemical Journal, 1981
- Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductaseArchives of Biochemistry and Biophysics, 1979
- Chemical and enzymic properties of riboflavin analogsBiochemistry, 1978
- Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivityBiochemistry, 1974