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- 14) TFA•Ahe-Phep(OPh)2; white solid; mp 223-225°C; IR νmax (KBr) cm−1 1593, 1545, 1491, 1261, 1205, 1186, 1137, 947; 1H-NMR (400 MHz, CD3OD) δH 0.96-1.09 (m, 2H), 1.29-1.45 (m, 4H), 2.01 (t, J=7.0, 2H), 2.65 (t, J=7.8, 2H), 2.92-3.01 (m, 1H), 4.93-5.01 (m, 1H), 7.07-7.30 (m, 15H); MALDI-TOF-MS (m/z) 467.7 (M+1)+.
- 15) Inactivation rate constants (kobs/[I]) were measured using the incubation method under pseudo-first-order reaction conditions. For chymotrypsin, the Ahe-Phe-phosphonate derivative (5 μM) was incubated with chymotrypsin (0.5 μM) in 40 mM Tris-HCl buffer containing 16 mM CaCl2 (pH 7.8) at 25°C. Portions, each of 300 μl, were withdrawn at 0.5, 5, 20, and 40 min after the start of incubation and mixed with the Tris-HCl buffer (2670 μl) and Bz-L-Tyr-pNA (30 μl, 60 μM) in DMSO to measure the remaining activities. For trypsin, the enzyme and Ahe-Phe-phosphonate concentrations were 0.4 μM and 320 μM, respectively, and Bz-Arg-pNA (100 μM) in DMSO was used as a substrate. Pseudo-first-order inactivation rate constants (kobs) were obtained from plots of ln vt/v0vs. time (triplicate experiments).
Bioscience, Biotechnology, and Biochemistry
Volume 66, 2002 - Issue 5