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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Simonetta M, Ansaloni A, Hanozet G M

Department of General Physiology and Biochemistry, University of Milan, Italy.

Comp Biochem Physiol B. 1979;64(4):363-7. doi: 10.1016/0305-0491(79)90283-9.

The effect of bile acids on the activity of liver alcohol dehydrogenase (L-ADH, EC 1.1.1.1) from different mammalian organisms is species dependent. 2. The kinetic behaviour of purified L-ADH from rat and rabbit liver in presence of deoxycholic acid and with ethanol as substrate shows two rather different patterns: for rabbit enzyme deoxycholic acid acts as a full competitive inhibitor, while for rat enzyme an activation effect is observed, with an increase of both Km and Vmax. Similar patterns are obtained with the steroid substrate 3 beta-hydroxy-5 beta-androstane-17one. 3. These results show that in some species, including man, L-ADH activity can be regulated by bile acids, that could control both ethanol oxidation and their own biosynthesis since L-ADH is involved in both metabolic pathways in liver cell.

胆汁酸对不同哺乳动物肝脏乙醇脱氢酶（L-ADH，EC 1.1.1.1）活性的影响具有物种依赖性。2. 以乙醇为底物，在脱氧胆酸存在的情况下，对来自大鼠和兔肝脏的纯化L-ADH的动力学行为进行研究，结果显示出两种截然不同的模式：对于兔酶，脱氧胆酸起完全竞争性抑制剂的作用，而对于大鼠酶，则观察到激活作用，同时Km和Vmax均增加。用甾体底物3β-羟基-5β-雄甾烷-17-酮也得到了类似的模式。3. 这些结果表明，在包括人类在内的某些物种中，L-ADH活性可受胆汁酸调节，胆汁酸既能控制乙醇氧化，又能控制其自身的生物合成，因为L-ADH参与肝细胞的这两种代谢途径。

Simonetta M, Ansaloni A, Hanozet G M

Department of General Physiology and Biochemistry, University of Milan, Italy.

Comp Biochem Physiol B. 1979;64(4):363-7. doi: 10.1016/0305-0491(79)90283-9.

The effect of bile acids on the activity of liver alcohol dehydrogenase (L-ADH, EC 1.1.1.1) from different mammalian organisms is species dependent. 2. The kinetic behaviour of purified L-ADH from rat and rabbit liver in presence of deoxycholic acid and with ethanol as substrate shows two rather different patterns: for rabbit enzyme deoxycholic acid acts as a full competitive inhibitor, while for rat enzyme an activation effect is observed, with an increase of both Km and Vmax. Similar patterns are obtained with the steroid substrate 3 beta-hydroxy-5 beta-androstane-17one. 3. These results show that in some species, including man, L-ADH activity can be regulated by bile acids, that could control both ethanol oxidation and their own biosynthesis since L-ADH is involved in both metabolic pathways in liver cell.

胆汁酸对不同哺乳动物肝脏乙醇脱氢酶（L-ADH，EC 1.1.1.1）活性的影响具有物种依赖性。2. 以乙醇为底物，在脱氧胆酸存在的情况下，对来自大鼠和兔肝脏的纯化L-ADH的动力学行为进行研究，结果显示出两种截然不同的模式：对于兔酶，脱氧胆酸起完全竞争性抑制剂的作用，而对于大鼠酶，则观察到激活作用，同时Km和Vmax均增加。用甾体底物3β-羟基-5β-雄甾烷-17-酮也得到了类似的模式。3. 这些结果表明，在包括人类在内的某些物种中，L-ADH活性可受胆汁酸调节，胆汁酸既能控制乙醇氧化，又能控制其自身的生物合成，因为L-ADH参与肝细胞的这两种代谢途径。