134423-82-8Relevant academic research and scientific papers
A Sensitive Fluorometric Assay for Activity of Pepsin
Yonezawa, Hiroo,Yamada, Kazuhiko,Uchikoba, Tetsuya,Kaneda, Makoto
, p. 2653 - 2658 (2007/10/02)
Fluorogenic substrates of pepsin; Dns-Ala-Ala-Phe-Trp-Val-Leu-OCH2Py (I), Ala-Ala-Trp-Phe-Leu-NHNHDns (II), and Ala-Ala-Trp-Phe-NHNHDns (III) were synthesized by a solution method and their properties were compared with Dns-Ala-Phe-Trp-Val-Leu-OCH2Py (IV)
Fluorogenic Substrate of Pepsin
Yonezawa, Hiroo,Izumiya, Nobuo
, p. 1407 - 1409 (2007/10/02)
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.
