Fluorimetric Assay of α-Chymotrypsin

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The enzymolysis by α-chymotrypsin of the substrates, N-acetyl-L-tryptophane ethyl ester and N-acetyl-L-tyrosine ethyl ester, was followed by means of fluorescence whose intensity increased fourfold and threefold 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/1. In such solutions the rate of esterolysis could be followed … continued below

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Bielski, Benon H. J. & Freed, Simon February 25, 1963.

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The enzymolysis by α-chymotrypsin of the substrates, N-acetyl-L-tryptophane ethyl ester and N-acetyl-L-tyrosine ethyl ester, was followed by means of fluorescence whose intensity increased fourfold and threefold 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/1. In such solutions the rate of esterolysis could be followed with the enzyme at 10-11 M/1.

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  • February 25, 1963

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  • Feb. 5, 2022, 9:55 a.m.

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Bielski, Benon H. J. & Freed, Simon. Fluorimetric Assay of α-Chymotrypsin, report, February 25, 1963; Washington D.C.. (https://digital.library.unt.edu/ark:/67531/metadc1255820/: accessed July 13, 2025), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT Libraries Government Documents Department.

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