IN VIVO AND VITRO REGULATION OF ACETALDEHYDE METABOLISM

线粒体乙醛脱氢酶是一种四聚体酶，但 在二价离子存在的情况下，能不能转化为更多的 活性二聚酶。胞液酶不被激活。的基础 不同生理浓度的镁和钙的反应差异 离子将用马的肝酶进行研究。实验以实现 确定该酶的体内状态将在大鼠和 牛肝线粒体酶。这些研究将包括使用in 体内抑制剂和分离的酶的体外杂交。这个 线粒体醛浓度之间的相互关系 将测定肝脏中的脱氢酶和乙醛代谢率 含有部分失活的乙醛脱氢酶的切片。一个 不同丙戊醇对该酶抑制方式的研究 衍生品将被用于开发潜在的自杀或 亲和力抑制剂。最后，酒精对肝脏同工酶的影响 乙醛脱氢酶的模式和分子聚集将是 在依赖酒精的大鼠身上确定。

Mitochondrial aldehyde dehydrogenase is isolated as a tetrameric enzyme but can in the presence of divalent ion cations be transformed into a more active dimericenzyme. Cytosolic enzymes are not activated. The basis for the differences in response to physiological concentrations of Mg2+ and Ca+ ions will be investigated with horse liver enzymes. Experiments to determine the in vivo state of the enzyme will be performed with rat and beef liver mitochondrial enzymes. These studies will include the use of in vivo inhibitors and in vitro hybridization of the isolated enzyme. The interrelationships between the concentration of mitochondrial aldehyde dehydrogenase and rates of aldehyde metabolism will be determined in liver slices which contain partially inactivated aldehyde dehydrogenase. An investigation of the mode of inhibition of the enzyme by various propargyl derivatives will be undertaken in order to develop potential suicide or affinity inhibitors. Lastly, the effect of alcohol on the liver isozyme pattern and molecular aggregation of aldehyde dehydrogenase will be determined in rats made dependent upon alcohol.