The effect of pre-incubation on trypsin kinetics at low pH.
A possible source of discrepancy between kinetic and spectroscopic studies of the active site ionizations in the enzyme trypsin (EC 3.4.21.4) could arise if a slow pH-dependent conformational change affected the rates at low pH. No such effect is observed within the time range of 1 min- 3 h when pre-incubation of trypsin at pH 2.0 or at pH 6.9 precedes the enzymatic hydrolysis of Nalpha-carbobenzoxy-L-lysine-p-nitrophenyl ester. The deacylation rate of this hydrolysis depends on a single pKa on the enzyme between pH 3 and pH 7.
D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011485:Protein Binding; D013997:Time Factors; D014357:Trypsin / Q000378:metabolism*
D014357:Trypsin