. Biological structure and function; proceedings. Biochemistry; Cytology. 50 C. H. W. HIRS, M. HALMANN, J. H. KYCIA permitted the evaluation of a pseudo first-order rate constant of o-oio min.~^ (on the basis of decimal logarithms) for the inactivation reaction. The results are represented graphically in Fig. 2, in which the difference in time scale for the lysine and activity values are occasioned by the dif- ference of 2 minutes in the lag phases observed for the dinitrophenylation and inactivation reactions. The agreement in the values is probably to some extent fortuitous in view of the us
. Biological structure and function; proceedings. Biochemistry; Cytology. 50 C. H. W. HIRS, M. HALMANN, J. H. KYCIA permitted the evaluation of a pseudo first-order rate constant of o-oio min.~^ (on the basis of decimal logarithms) for the inactivation reaction. The results are represented graphically in Fig. 2, in which the difference in time scale for the lysine and activity values are occasioned by the dif- ference of 2 minutes in the lag phases observed for the dinitrophenylation and inactivation reactions. The agreement in the values is probably to some extent fortuitous in view of the usual errors that obtain in the. 10 J I L J \ L 80 10 20 40 60 MINUTES Fig. 2. Kinetics of inactivation of ribonuclease A by dinitrophenylation. Conditions were the same as described in Table I. For the significance of the lysine values, see the text. determination of lysine and the problems involved in removing excess reagent before undertaking the measurement of ribonuclease activity. The values for the constant nevertheless furnish quantitative evidence that the substitution of a single e-amino group is capable of inactivating the enzyme. The powerful inhibition effected by the nucleotides and pyrophosphate ion suggest that the e-amino group in question is located at either the binding or catalytic site of the molecule. It is likely that other groups essential to the activity of the enzyme are among those that become substituted much more slowly at pH 8 through. 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 IUB/IUBS International Symposium (1st : 1960 : Stockholm); International Union of Biochemistry; International Union of Biological Sciences; Goodwin, T. W. (Trevor Walworth); Lindberg, Olov, 1914-. London, New York, Academic Press
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