Studies on the interaction between disulfiram and sheep liver cytoplasmic aldehyde dehydrogenase.
Studies on the interaction between disulfiram and sheep liver cytoplasmic aldehyde dehydrogenase.
复制标题
双硫仑与羊肝细胞质醛脱氢酶相互作用的研究
作者：
T. Kitson
本文研究了二硫胺、[1-14C]二硫胺等硫醇试剂对绵羊肝脏胞质乙醛脱氢酶活力的影响。这一结果与双硫兰与酶之间的快速共价相互作用是一致的，与双硫兰是胞质乙醛脱氢酶的可逆竞争抑制剂的观点不一致。酶活力损失约90%与二硫胺加入量之间存在非线性关系，并对其可能原因进行了讨论。剩下的大约。10%的活性对双硫兰相对不敏感。结果发现，每个四聚体酶分子中只有少量基团(一到两个)的修饰是导致观察到的活性丧失的原因。双硫胺对脱氢酶活性的影响比对酯酶活性的影响更大。带负电荷的硫醇试剂对细胞质中的乙醛脱氢酶几乎没有影响。2，2‘-二硫代联吡啶是该酶的激活剂。
The effect of disulfiram, [1-14C]disulfiram and some other thiol reagents on the activity of cytoplasmic aldehyde dehydrogenase from sheep liver was studied. The results are consistent with a rapid covalent interaction between disulfiram and the enzyme, and inconsistent with the notion that disulfiram is a reversible competitive inhibitor of cytoplasmic aldehyde dehydrogenase. There is a non-linear relationship between loss of about 90% of the enzyme activity and amount of disulfiram added; possible reasons for this are discussed. The remaining approx. 10% of activity is relatively insensitive to disulfiram. It is found that modification of only a small number of groups (one to two) per tetrameric enzyme molecule is responsible for the observed loss of activity. The dehydrogenase activity of the enzyme is affected more severely by disulfiram than is the esterase activity. Negatively charged thiol reagents have little or no effect on cytoplasmic aldehyde dehydrogenase. 2,2'-Dithiodipyridine is an activator of the enzyme.