Meijer A J, van Woerkom G M, Williamson J R, Tager J M
Biochem J. 1975 Aug;150(2):205-9. doi: 10.1042/bj1500205.
The oxidation of ethanol by isolated liver cells from starved rats is limited by the rate of removal of reducing equivalents generated in the cytosol by alcohol dehydrogenase. Evidence is presented suggesting that, in these cells, transfer of reducing equivalents from the cytosol to the mitochondria is regulated by the intracellular concentrations of the intermediates of the malate-aspartate and glycerol 3-phosphate cycles, as well as by flux through the respiratory chain. In liver cells isolated from fed rats, the availability of substrate increased the cell content of intermediates of the hydrogen-transfer cycles, and enhanced ethanol uptake. Under these conditions, ethanol consumption is limited by the availability of ADP for oxidative phosphorylation.
饥饿大鼠分离出的肝细胞对乙醇的氧化作用受酒精脱氢酶在胞质溶胶中产生的还原当量的去除速率限制。有证据表明,在这些细胞中,还原当量从胞质溶胶向线粒体的转移受苹果酸 - 天冬氨酸循环和3 - 磷酸甘油循环中间体的细胞内浓度以及呼吸链通量的调节。在从喂食大鼠分离出的肝细胞中,底物的可利用性增加了氢转移循环中间体的细胞含量,并增强了乙醇摄取。在这些条件下,乙醇消耗受用于氧化磷酸化的ADP的可利用性限制。