Abdallah M A, Biellmann J F, Lagrange P
Biochemistry. 1979 Mar 6;18(5):836-8. doi: 10.1021/bi00572a015.
A stopped-flow spectrophotometer was modified so that the volumes to be mixed were in a ratio of 1:50. Using this instrument, we have shown that the effective substrate in the reduction of acetaldehyde catalyzed by horse liver alcohol dehydrogenase was the carbonyl form of acetaldehyde and that the enzyme does not catalyze the dehydration of the hydrated form of acetaldehyde. Unlike trifluoroacetaldehyde hydrate, which is a competitive inhibitor with respect to ethanol, acetaldehyde hydrate did not inhibit the enzymatic reaction at concentrations as high as 60 mM.
对一台停流分光光度计进行了改装，使得混合的体积比为1:50。使用这台仪器，我们已经表明，在马肝醇脱氢酶催化的乙醛还原反应中，有效的底物是乙醛的羰基形式，并且该酶不催化乙醛水合物的脱水反应。与水合三氟乙醛（它是乙醇的竞争性抑制剂）不同，乙醛水合物在浓度高达60 mM时并不抑制酶促反应。
