Bulletin of the Chemical Society of Japan p. 1407 - 1409 (1991)
Update date:2022-08-03
Topics:
Yonezawa, Hiroo
Izumiya, Nobuo
Fluorogenic substrates of pepsin; Dns-Ala-Phe-Trp-Val-Leu-OCH2Py and Dns-Phe-Trp-Val-Leu-OCh2Py were synthesized by a solution method.Incubation of pepsin with Dns-Ala-Phe-Trp-Val-Leu-OCH2Py resulted in specific cleavage at the Phe-Trp bond and the time-dependent increase in fluorescence intensity at 345 nm paralleling the extent of substrate hydrolysis.The optimum pH of the substrate was 3.0 and Km and kcat values were 8.0x10-5 M and 0.10 s-1, respectively.The linearity of the plot of fluorescence intensity vs. enzyme concentration was satisfactory in the range of 50 nM to 500 nM of pepsin at a substrate concentration of 50 μM.Because of its simplicity and rapidity, this method is useful for the measurement of pepsin action.In contrast, Dns-Phe-Trp-Val-Leu-OCH2Py was not cleaved by pepsin.
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