IN VIVO AND VITRO REGULATION OF ACETALDEHYDE METABOLISM

线粒体醛脱氢酶作为四聚体酶分离， 在二价阳离子存在下， 活性二聚酶 胞质酶未被激活。 的基础 不同生理浓度的Mg ~（2+）和Ca ~（2+） 离子将用马肝酶进行研究。 实验来 确定酶的体内状态将用大鼠进行， 牛肝线粒体酶。 这些研究将包括在 分离的酶的体内抑制剂和体外杂交。 的 线粒体乙醛浓度与 脱氢酶和醛代谢率将在肝脏中测定 含有部分失活的醛脱氢酶的切片。 一个 不同炔丙基对酶的抑制方式的研究 衍生物将进行，以发展潜在的自杀或 亲和抑制剂。 最后，研究了酒精对肝脏同工酶的影响 醛脱氢酶的模式和分子聚集， 在依赖酒精的大鼠中测定。

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.