Abstract
AbstractThe quantum yield of inactivation of chymotrypsin was found to be independent of variations in conditions of irradiation including light intensity, concentration of the irradiated solution, rate of stirring and the presence or absence of oxygen. The quantum yield for inactivation is at a minimum at the isoelectric point (pH 5.4). An explanation is offered for the variation of the quantum yield with pH in terms of an internal Franck‐Rabinowitch mechanism. The absorption spectra of the enzyme was also studied as a function of pH, as was that of an amino acid mixture whose composition corresponded to that of chymotrypsin. Evidence is presented for the existence of bound, un‐ionizing tyrosine in the native enzyme and of unbound tyrosine in alkali‐denatured enzyme. The significance of changes in the absorption spectra accompanying irradiation is discussed.
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