The reaction of yeast alcohol dehydrogenase with iodoacetamide as determined with a silver-silver iodide electrode

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Abstract
The reaction of yeast alcohol dehydrogenase with iodoacetamide was investigated by measuring the I- ions produced by means of a silver-silver-iodide electrode. One thiol group/active site reacted rapidly with iodoacetamide. A large number of other groups reacted in the presence of high concentrations of anionic detergent. The initial rate of reaction of the enzyme with iodoacetamide was independent of pH over the range 4[long dash]9. The rate fell off below pH 4. NADH, and to a lesser extent NAD+, protected the enzyme against iodoacetamide. Ethanol was without effect. The enzyme was inhibited by very low concentrations of Ag+ ions which labilized the protein towards iodoacetamide and interfered with the binding of coenzynmes.