Abstract
Summary: The mechanism of mercury inhibition of invertase, β-d-fructofuranoside-fructohydrolase EC. 3.2.1.26, from Saccharomyces cerevisiae, both in vitro and in vivo, is similar with respect to effective mercury concentrations. Contrary to previous reports on invertase from S. cerevisiae, the enzyme in this study does not dimerize in the presence of mercury nor does it exhibit competitive inhibition kinetics. A further apparent inconsistency with previous work is the marked dependency of inhibition upon pH and anion concentrations.
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