An enzymatic fluorimetric assay for myo-inositol.
L C MacGregor, F M Matschinsky
Index: Anal. Biochem. 141(2) , 382-9, (1984)
Full Text: HTML
Abstract
An enzymatic assay for myo-inositol (MI) is described. The method is based on the oxidation of MI by NAD+-dependent myo-inositol dehydrogenase, coupled to reoxidation of NADH with oxalacetate and malate dehydrogenase. The resultant malate is measured fluorimetrically. Several variations of the assay are described for measuring MI in serum and in tissues in amounts ranging from 0.2 pmol to 8 nmol. Highest sensitivity is achieved by applying an oil-well technique for handling small droplets, and by using the principle of enzymatic cycling. The potential of the technique is illustrated by MI measurements in several tissues of normal and diabetic rats and Chinese hamsters.
Related Compounds
Related Articles:
1986-10-01
[Anal. Biochem. 158(1) , 59-63, (1986)]
1966-02-25
[J. Biol. Chem. 241(4) , 800-6, (1966)]
1956-02-01
[Arch. Biochem. Biophys. 60(2) , 352-63, (1956)]
1987-01-01
[Free Radic. Res. Commun. 4(2) , 105-8, (1987)]
1984-03-22
[Biochim. Biophys. Acta 798(1) , 88-95, (1984)]