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- W2093202384 abstract "The enzyme-catalyzed hydrolysis of peptide and amide substrates results in the generation of ionic species which in turn lead to a change in the electrical conductivity of the reaction medium. By recording this physical property it is possible to study the kinetics of the hydrolytic reactions. The principle of the conductometric method is given and its application to the assay of proteolytic enzymes is illustrated by a number of reactions catalyzed by chymotrypsin Aα (EC 3.4.21.1) and trypsin (EC 3.4.21.4). The measured signal is related to product concentration by the molar conductivity coefficient (Λb). The measurement of this coefficient is described; it is shown to vary with the experimental conditions, particularly when different buffer systems are used. The kinetic results (i.e., values of kcat and Km) for the chymotrypsin Aα and trypsin-catalyzed hydrolysis of a number of specific peptide and amide substrates are given. The results agree closely with previously published values obtained using a number of other assay techniques." @default.
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- W2093202384 date "1982-02-01" @default.
- W2093202384 modified "2023-09-27" @default.
- W2093202384 title "A conductometric method for the assay of amidase and peptidase activities" @default.
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- W2093202384 doi "https://doi.org/10.1016/0003-2697(82)90332-3" @default.
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