. Currents in biochemical research, 1956; twenty-seven essays charting the present course of biochemical research and considering the intimate relationship of biochemistry to medicine, physiology, and biology. Biochemistry -- Research. HUGO THEORELL general phenomenon, since it does not occur in yeast ADH, triosephosphate, or glutamic dehydrogenases. The displacement of the band enabled us to establish spec- trophotometrically that 1 mol ADH binds 2 mols of DPNH. For the sake of convenience we shall denote V2 ADH as ADH'. Furthermore, by using rapid spectrophotometry Theorell and Chance (24) c
. Currents in biochemical research, 1956; twenty-seven essays charting the present course of biochemical research and considering the intimate relationship of biochemistry to medicine, physiology, and biology. Biochemistry -- Research. HUGO THEORELL general phenomenon, since it does not occur in yeast ADH, triosephosphate, or glutamic dehydrogenases. The displacement of the band enabled us to establish spec- trophotometrically that 1 mol ADH binds 2 mols of DPNH. For the sake of convenience we shall denote V2 ADH as ADH'. Furthermore, by using rapid spectrophotometry Theorell and Chance (24) could determine the velocity of the band J/o 320 330 J-^O 350 Fig. 5. Millimolar extinction of free and ADH-bound DPNH. Ordinate: e X mM-i. (From ref. 23.) and thus obtained the value 4 X 10^ M~^ ;^ for the velocity constant (ki) of the combination between DPNH and ADH. In the equilibrium [DPNH][CH3CHO][H+] [DPNJlCaHeOH] Racker (15), using small amounts of yeast ADH, had found K to be constant and independent of pH, as required by the formula. The value for K was close to 10~". Since iT is a function of purely thermodynamic parameters, it was no surprise that we found the same value with low concen- trations of liver ADH. But in the liver the concentration of the enzyme (^ 1 g. per kilogram wet weight) is not at all low enough to be negligible. 294. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Green, David Ezra, 1910-. New York, Interscience Publishers
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