Add time:09/03/2019         Source:sciencedirect.com

Publisher SummaryThis chapter describes a continuous spectrophotometric assay and purification of D-tagatose-6-phosphate kinase that is based on coupling adenosine diphosphate (ADP) formation to pyruvate kinase and lactate dehydrogenase. This is an inducible enzyme that is instrumental in the catabolism of lactose and D-galactose in Staphylococcus aureus. With the coupling enzymes in excess, the rate of ADP formation is equivalent to the rate of NADH oxidation, which is measured by the absorbance decrease at 340 nm. The purification procedure involves several steps, such as growth of organism, preparation of cell extracts, bentonite treatment, diethylaminoethyl (DEAE)-cellulose chromatography I, DEAE-cellulose chromatography II, hydroxyapatite chromatography, and Sephadex G-100 chromatography. The subunit molecular weight is estimated to be 52,000 and the native enzyme is a dimer. D-Tagatose 6-phosphate is the natural substrate and several nucleoside triphosphates can serve as phosphoryl donors. Activity as a function of pH is maximal at about pH 8.5 in glycylglycine buffer.

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