PURIFICATION AND SOME PROPERTIES OF L-GLYCOL DEHYDROGENASE FROM HEN MUSCLE

An enzyme which catalyzes the NAD(P)H-linked reversible reduction of uncharged vicinal dicarbonyls and .alpha.-hydroxycarbonyls to L-(+)-glycols was purified from hen''s muscle. This enzyme has not been previously described. 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. Three forms of this enzyme differing in PI were isolated; 2 forms, which together represent about 90% of total recovered activity, are electrophoretically pure. MW, pH profiles and affinity for substrates are also described.