Add time:09/25/2019         Source:sciencedirect.com

Publisher SummaryThis chapter discusses the determination of L-Fuculose (cas 13074-08-3) 1-Phosphate aldolase. L-fuculose 1-phosphate aldolase is assayed by determination of dihydroxyacetone phosphate with glycerol 1-phosphate dehydrogenase and reduced diphosphopyridine nucleotide DPNH; the amount of DPNH utilized is measured spectrophotometrically at 340 mμ and is proportional to dihydroxyacetone phosphate in the mixture. Because of the presence of DPNH oxidase in the cruder preparations, these fractions are assayed in two steps: the aldolase preparation is incubated with L-fuculose 1-phosphate, and after inactivation of the enzyme, dihydroxyacetone phosphate is determined in an aliquot. In more purified preparations (Ammonium Sulfate Fraction), the amounts of contaminating enzymes have been sufficiently reduced to permit coupling of the aldolase reaction directly with the glycerol 1-phosphate dehydrogenase system; the rate of formation of dihydroxyacetone phosphate is determined spectrophotometrically in a continuous manner. L-Fuculose 1-phosphate aldolase is essentially specific for L-fuculose 1-phosphate. Optimal activity of the enzyme is obtained in the range from pH 6.9 to 7.2; approximately 50% of the maximal activity is observed at pH 6.5 and 8.

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