The Journal of Iryestioatiye Dermatology
نویسنده
چکیده
The materials and general analytical methods have been described in some detail in a preceding communication (1). The assay method for a-glyeerophosphate dehydrogenase was essentially the same as that of Lowry and Passonneau (2). Since this enzyme catalyzes NADH-coupled reaction with dihydroxyacetone phosphate as substrate, one of the products, NAD2, may be measured with a sonsitive fluorometer. Dihydroxyacetone phosphate was obtained commercially as monocyclobexylamine salt, dimethyl ketal }IO (molecular weight n 432). It was converted to free acid by Dowex 50 (H) resin and the resulting acid solution was kept at 38° C for 4 hours to hydrolyze the ketal. The acid solution was stored at —20° C and neutralized just before use. The concentration of the dihydroxyacetone phosphate solution was measured by an enzymatic method, i.e., the disappearance of NADH was followed in the Beckman spectrophotometer at 340 mji using the following mixture: 0.15 mie NADH; 20 jig crystalline a-glycerophospbate dehydrogenase; 0.1 Iii Tris-HC1 buffer, pH 7.5; and approximately 0.1 to
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