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By Jesse P. Greenstein, John T. Edsall

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Spackman, D . , Stein, W. , and Moore, S. (1960). J. Biol. , in press. Tanford, C , and Hauenstein, J. D . (1956). / . Am. Chem. Soc. 78, 5287. Tanford, C , and Weber, R. E . (1960), in press. Tanford, C , Hauenstein, J. , and Rands, D . G. (1955). J. Am. Chem. Soc 77, 6409. Considerations of the Structure and Function of Carboxypeptidase A1 HANS NEURATH, JOHN A. RUPLEY, and BERT L. VALLEE Department of Biochemistry, University of Washington, Seattle, Washington, and the Biophysics Research Laboratory of the Department of Medicine, Harvard Medical School, Peter Bent Brig· ham Hospital, Boston, Massachusetts A N IMPORTANT PHASE of Jesse Greenstein's scien­ tific work has dealt with the action of stereospecific enzymes on isomeric amino acids and peptides.

Effect of Deuterium on the Transition Temperature If deuterium is substituted for hydrogen, and the latter is in­ volved in a hydrogen bond, then the bond strength will be affected. As a consequence one would expect a deuterated helical macromolecule to have a different stability from a hydrogen-containing one, using the random coil as a reference state. This altered stability should manifest itself in a change in the transition temperature between the helix and random coil. , 1959). Since ribonuclease shows a transition with increasing temperature (Harrington and Schellman, 1956), the effect of deuterium substitution on the transition temperature was investi­ gated by means of optical rotation measurements in order to obtain additional evidence for the existence of internal hydrogen bonds in ribonuclease.

No change in sedimentation behavior was observed, in con­ trast to similar studies with other metalloenzymes such as glutamic dehydrogenase, studied by Frieden (1958), and yeast alcohol de- STRUCTURE AND FUNCTION OF CARBOXYPEPTIDASE 5 6 7 8 9 pH of Buffer 10 55 II FIG. 10. 3 ionic strength. The open squares denote the minor component of the metal-free protein. ) hydrogenase, studied by Kägi (1959), who, under these conditions, found dissociation of these metalloenzymes into smaller components. Measurements of the optical rotation over a wide pH range have likewise failed to reveal significant differences between native and metal-free protein.

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