Figure 2.
Fig. 2. A, the pH rate profiles for the reaction of
prolyl oligopeptidase with the octapeptide. The reactions were
performed in the presence ( ) and
absence ( circle )
of 0.5 M NaCl. The broken lines calculated from Equation 1 stand
for the two pH-dependent forms in the presence of 0.5 M NaCl. B,
formation of enzyme-inhibitor complex as a function of pH. The
association constants (1/K[i]) were calculated from Equation 3
for prolyl oligopeptidase and Z-Gly-Pro-OH in the presence (
) and
absence ( circle )
of 0.5 M NaCl. First-order rate constants were measured with
2-20 nM enzyme and 0.29 µM Z-Gly-Pro-Nap as substrate.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
1262-1266)
copyright 2001.
) and
absence ( 
circle )
of 0.5 M NaCl. The broken lines calculated from Equation 1 stand
for the two pH-dependent forms in the presence of 0.5 M NaCl. B,
formation of enzyme-inhibitor complex as a function of pH. The
association constants (1/K[i]) were calculated from Equation 3
for prolyl oligopeptidase and Z-Gly-Pro-OH in the presence (