Bijleveld C, Vaartjes W J, Geelen M J
Laboratory of Veterinary Biochemistry, University of Utrecht, The Netherlands.
Horm Metab Res. 1989 Nov;21(11):602-5. doi: 10.1055/s-2007-1009298.
Acetyl-CoA carboxylase activity was measured in digitonin-permeabilized rat hepatocytes by coupling the carboxylase reaction to the fatty acid synthase reaction. Using this assay the activity of acetyl-CoA carboxylase was covariant with the rate of fatty acid synthesis. Insulin and the tumor promotor phorbol myristate acetate were found to stimulate, and glucagon and noradrenaline to inhibit both cellular parameters. The stimulation of acetyl-CoA carboxylase by insulin developed slowly (15 to 30 min) whereas the phorbol myristate acetate effect developed faster (within 15 min). The inhibition of the enzyme caused by glucagon was already apparent within 1 min after hormone addition. Inhibition by noradrenaline, in the presence of propranolol, was also quite rapid and occurred within 2 min after addition of the agonist.
通过将羧化酶反应与脂肪酸合酶反应偶联,在洋地黄皂苷通透的大鼠肝细胞中测量乙酰辅酶A羧化酶活性。使用该测定法,乙酰辅酶A羧化酶的活性与脂肪酸合成速率呈协变关系。发现胰岛素和肿瘤促进剂佛波酯肉豆蔻酸酯可刺激这两个细胞参数,而胰高血糖素和去甲肾上腺素则抑制它们。胰岛素对乙酰辅酶A羧化酶的刺激作用发展缓慢(15至30分钟),而佛波酯肉豆蔻酸酯的作用发展较快(15分钟内)。添加激素后1分钟内,胰高血糖素对该酶的抑制作用就已明显。在普萘洛尔存在的情况下,去甲肾上腺素的抑制作用也相当迅速,在添加激动剂后2分钟内就会出现。