Abstract
An enzyme capable of hydrolyzing pyruvic oxime to hydroxylamine and pyruvic acid has been purified 14-fold from extracts of the ciliated protozoan, Tetrahymena pyriformis. The enzyme also hydrolyzes α-ketoglutaric oxime at all stages of purification. Activity toward pyruvic oxime is inhibited by small amounts of zinc, cobaltous and ferric ions, as well as by azide. High concentrations of potassium, magnesium, and calcium ions are also inhibitory. Enzymic activity is unaffected by high concentrations of sodium or cuprous ions, or by iodoacetate or p-chloromercuriphenylsulfonic acid. The enzyme shows optimal activity over the pH range 6.1–7.8.
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