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

被引：14

作者：

BERNARDO, A ^{[1
]}

BURGOS, J ^{[1
]}

MARTIN, R ^{[1
]}

机构：

[1] FAC VET LEON, BIOCHEM & FOOD TECHNOL LAB, LEON, SPAIN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1981年 / 659卷 / 01期

关键词：

D O I：

10.1016/0005-2744(81)90283-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：189 / 198

页数：10