. 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. FRANK M. HUENNEKENS affinity, or binding, of the two components, remains obscure. Other quantitative data, such as the variation in binding with pH, ionic strength, and temperature, are noticeably lacking. There remain only fragmentary, qualitative observations based upon chemical modification of the coenzyme or protein. These studies are similar in rationale to
. 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. FRANK M. HUENNEKENS affinity, or binding, of the two components, remains obscure. Other quantitative data, such as the variation in binding with pH, ionic strength, and temperature, are noticeably lacking. There remain only fragmentary, qualitative observations based upon chemical modification of the coenzyme or protein. These studies are similar in rationale to the search for the active center of certain proteolytic enzymes, where the broad specificity of the enzyme permits a variety of structurally similar substrates to be used and the variation in reaction kinetics noted. Unfortu- nately, the problem is somewhat analogous to the use of quantum mechanical methods to relate absorption spectra to structure of complex organic molecules; the correlation becomes more exact in proportion to the a priori knowledge of both factors. Some very interesting observations have been made re- cently by Racker, Velick, Boyer, and Chance on the binding of DPN by 3-phosphoglyceraldehyde dehydrogenase (35). It has been suggested that the nicotinamide portion of DPN is bound to a glutathione residue of the protein, as shown below. ENZYME Whether or not this tentative structure is correct, it is known that combination of DPN and the enzyme gives rise to a new absorp- tion band at 360 m/x. By contrast, reduced DPN forms a spec- troscopic complex (Xn,ax ^t 325 mn) with horse liver alcohol dehydrogenase or lactic dehydrogenase, but neither complex is observed with glutamic dehydrogenase or yeast alcohol dehy- drogenase. The question has been raised repeatedly whether 512. 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 perfec
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