Kitson T M
Biochem J. 1979 Dec 1;183(3):751-3. doi: 10.1042/bj1830751.
Small concentrations of 2,2'-dithiodipyridine cause a rapid activation of sheep liver cytoplasmic aldehyde dehydrogenase in the presence of NAD+. Enzyme pre-modified by 2,2'-dithiodipyridine is largely protected against the potent inactivatory effect of disulfiram. 2,2'-Dithiobis-(5-nitropyridine) inactivates the enzyme. The implications of these results are discussed with reference to various possible classes of thiol group in aldehyde dehydrogenase.
在烟酰胺腺嘌呤二核苷酸(NAD⁺)存在的情况下,低浓度的2,2'-二硫代二吡啶会使绵羊肝脏细胞质醛脱氢酶迅速活化。经2,2'-二硫代二吡啶预先修饰的酶在很大程度上可免受双硫仑的强效失活作用影响。2,2'-二硫代双(5-硝基吡啶)会使该酶失活。本文参照醛脱氢酶中各种可能的巯基类别对这些结果的意义进行了讨论。