Purification and some properties of L-glycol dehydrogenase from hen's muscle

Biochim Biophys Acta. 1981 May 14;659(1):189-98. doi: 10.1016/0005-2744(81)90283-7.

Abstract

1. An enzyme which catalyzes the NAD(P)H-linked reversible reduction of uncharged vicinal dicarbonyls and alpha-hydroxycarbonyls to L-(+)-glycols has been purified from hen's muscle. This enzyme has not been previously described. 2. According to the rules of the I.U.P.A.C.-I.U.B. Enzymes Commission, the systematic name of L-(+)-glycol:NAD(P) oxidoreductase and the trivial name of L-glycol dehydrogenase are proposed for the enzyme. 3. Three forms of this enzyme differing in pI have been isolated; two forms, which together represent about 90% of total recovered activity, and electrophoretically pure. 4. Molecular weight, pH profiles and affinity for substrates are also described.

MeSH terms

  • Acetoin / metabolism
  • Alcohol Oxidoreductases / isolation & purification*
  • Animals
  • Butylene Glycols / metabolism
  • Chickens
  • Female
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing
  • Molecular Weight
  • Muscles / enzymology*
  • NADP / metabolism
  • Substrate Specificity

Substances

  • Butylene Glycols
  • NADP
  • Acetoin
  • Alcohol Oxidoreductases
  • L-glycol dehydrogenase