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- W2461538025 endingPage "1947" @default.
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- W2461538025 abstract "The analysis of the pH-dependence of Michaelis constant and maximal velocity for the reaction catalyzed by beta-D-hexosaminidase from Halocynthia roretzi revealed two essential ionazable groups of the enzyme. One of them controls substrate binding and has a pKa of 5.5 in free enzyme. The other group (pKa=5.6) is necessary for the occurrence of the catalytic step and appears not to change its pKa on substrate binding." @default.
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- W2461538025 date "1976-11-01" @default.
- W2461538025 modified "2023-09-22" @default.
- W2461538025 title "[Effect of pH on the kinetics of the reaction catalyzed by beta-D-hexosaminidase from Halocynthia roretzi]." @default.
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