转移酶
酶
生物化学
细胞培养
污渍
分子生物学
酶分析
辅酶A
免疫沉淀
谷胱甘肽S-转移酶
甲基转移酶
末端脱氧核苷酸转移酶
化学
蛋氨酸
细胞
生物
还原酶
氨基酸
基因
谷胱甘肽
细胞凋亡
标记法
遗传学
甲基化
作者
Wei Zhang,Ronald Lindahl,Perry F. Churchill
出处
期刊:PubMed
日期:1990-09-15
卷期号:50 (18): 5858-62
被引量:7
摘要
The regulation of succinyl-CoA:acetoacetyl-CoA transferase (CoA transferase) has been studied in 8 rat hepatoma cell lines. Compared with normal rat hepatocytes, which have almost nondetectable activity of the enzyme, the hepatoma cell lines have a wide range of expression of CoA transferase activity, from as low as 45 nmol/min/mg to as high as 960 nmol/min/mg. Western blotting showed that the different levels of CoA transferase activity were due to differing amounts of the enzyme in the cells. This was further attributed to the varying amounts of the enzyme synthesized in the cells as monitored by L-[35S]methionine labeling followed by immunoprecipitation. To study further the differential expression of CoA transferase in the hepatoma cell lines, the relative quantity of functional CoA-transferase mRNA in the cells was measured by in vitro translation. The results showed that the levels of functional CoA transferase mRNA detected were consistent with the differences in the enzyme activity in the cells. Since CoA transferase is the key enzyme responsible for the utilization of ketone bodies as an alternative energy source, the expression of CoA transferase in hepatoma cells may play a role in energy production.
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