Abstract
1. 1. The pH dependence of the in-situ β-galactosidase activity has been investigated in the presence of the monovalent cations, Na +. K + and Li +. 2. 2. These cations induced some conformational changes in the enzyme molecule affecting to ionization of the prototropic groups that controlled the enzymatic activity. 3. 3. The rate of hydrolysis of o- nitrophenyl-β- d-galactopyranoside by β-galactosidase was increased, decreased or not affected by these cations depending of pH. 4. 4. Some differences with respect to β-galactosidase in vitro were observed.
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