1887

Abstract

An enzyme which oxidizes 1,2-propanediol in the presence of NADhas been purified from lysates of The enzyme was activated by monovalent cations, had a pH optimum between 9 and 10, and showed a substrate specificity unlike any known alcohol or glycerol dehydrogenase. The enzyme had an apparent of 17 m for 1,2-propanediol and 0.37 mM for NAD. When chromatographed on a Sephadex G-150 column, the enzyme eluted as a single peak in the molecular weight region of a bovine serum albumin marker. An antibody to the purified enzyme was prepared in goats. When antiserum was reacted with the enzyme in immunodiffusion experiments, a single precipitin band was detected. When the enzyme was mixed with an excess of antibody and then reacted with substrate, enzyme activity was completely inhibited.

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/content/journal/micro/10.1099/00221287-119-2-451
1980-08-01
2021-05-09
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