Abstract
The enzymic hydrolysis by α-chymotrypsin of the substrates, N-acetyl- l-tryptophan ethyl ester and N-acetyl- l-tyrosine ethyl ester, was followed by means of fluorescence whose intensity increased threefold and fourfold per mole, respectively, as substrate was transformed into amino acid. The assay by fluorescence was several orders of magnitude more sensitive than the assay by differential absorption spectra of these substances and was in agreement with it in those concentration regions where both methods overlap. To maintain linearity between concentration and fluorescence intensity, the concentration of substrate should be no greater than 10 −4 M. In such solutions the rate of ester hydrolysis could be followed with the enzyme at 10 −11 M.
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