. 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. PROSTHETIC GROUPS, COENZYMES AND ENZYMES. DPN ADH {2c) ADH i ADH—DPN + + G2H5OH {2d) C2H5OH The influence of some sodium salts of different anions on the reaction velocity in the ADH-system was studied and found to be unexpectedly large and interesting. Some values are sum- marized in Table IV. TABLE IV Influence of Some Sodium Salts, M, on the React
. 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. PROSTHETIC GROUPS, COENZYMES AND ENZYMES. DPN ADH {2c) ADH i ADH—DPN + + G2H5OH {2d) C2H5OH The influence of some sodium salts of different anions on the reaction velocity in the ADH-system was studied and found to be unexpectedly large and interesting. Some values are sum- marized in Table IV. TABLE IV Influence of Some Sodium Salts, M, on the Reaction Velocitv, V/e ;, IN THE ADH-DPN-DPNH System {pU = , ° G.) (ref. 28) [ADHM = CH3CHO] = 2100 mM DPNH] = [ADHM = mM [CjHsOH] = 2300 mM [DPN] = 8mM Salt V/e sec. -1 Salt V/e ' Glycine Phosphate Phosphate + Versene Chloride 15 Glycine Phosphate Chloride Sulfate Sulfate Nitrate Nitrate Bromide Bromide Formate Formate 0 Acetate We think very few people would have considered it likely to predict in advance that, for example, M NaBr would inhibit the aldehyde-DPNH reaction by 99%. In general, the table shows how careful we have to be in controlling the ionic milieu when dealing with coenzyme-enzyme reactions. M chloride and M formate were subjected to the more com- plete set of analyses that allowed calculations of all the six velocity constants (see Table III). M chloride decreases 303. 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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