Abstract
A triphosphopyridine nucleotide specific alcohol dehydrogenase was partially purified from cell-free extracts of L. mesenteroides. The enzyme is extremely unstable; the presence of cysteine in enzyme prepns. partially protects against loss of activity during fractionation. The properties exhibited by the enzyme differ in some respects from those reported for a wheat germ triphosphopyridine nucleotide alcohol dehydrogenase and from those descr. for diphosphopyridine nucleotide alcohol dehydrogenases from yeast or liver.