PubMed · 5910260
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1966-04-29. Ananase.. https://pubmed.ncbi.nlm.nih.gov/5910260/
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The kinetics of enzyme inactivation in aqueous solution of neutral pH were studied for alpha-chymotrypsin, bromelain, and kallikrein. Inactivation of alpha-chymotrypsin and bromelain followed simple first-order kinetics, and the rate constant obtained conformed to the Arrhenius relationship. Kallikrein, however, presented more complicated kinetics of inactivation, which could be described by a kinetic expression combining a reversible and an irreversible pathway. Nonlinear regression analysis suggested that the rate constants conform reasonably well to the Arrhenius relationship. The results suggest that inactivation of enzymes in aqueous solution can be modeled even if the profile is complicated and that the inactivation rates can be predicted based on the relationship between the parameter estimates and temperature.
1H- and 13C-NMR assignments for the carbohydrate part of the glycopeptide alpha-D-Man-(1----6)-[beta-D-Xyl-(1----2)]-beta-D-Man-(1----4)-beta-D- GlcNAc-(1----4)-[alpha-L-Fuc-(1----3)]-beta-D-GlcNAc-(1----N)-Asn approximately, derived from the proteolytic enzyme bromelain (EC 3.4.22.4), have been obtained using homo- and heteronuclear correlation spectroscopy, two-dimensional homonuclear Hartmann-Hahn and nuclear Overhauser enhancement experiments. A conformational model for the carbohydrate chain, deduced from the NMR data and consistent with hard-sphere exo-anomeric calculations shows that the rotamer population about the C-5--C-6 bond of beta-Man is restricted to the P omega = 180 rotamer, mainly.