Nakanishi S, Tanabe T, Horikawa S, Numa S
Proc Natl Acad Sci U S A. 1976 Jul;73(7):2304-7. doi: 10.1073/pnas.73.7.2304.
Specific polysomes involved the the synthesis of acetyl-CoA carboxylase [acetyl-CoA: carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] have been identified by the binding of 125I-labeled antiacetyl-CoA carboxylase to rat liver polysomes. The binding is highly specific and occurs through the recognition of the nascent peptide chains on polysomes. With the use of the 125I-labeled antibody binding technique, it has been demonstrated that the relative content of acetyl-CoA carboxylase-synthesizing polysomes in the liver correlates well with the rate of hepatic synthesis of the enzyme in rats subjected to different dietary conditions as well as in alloxan-diabetic rats with or without insulin treatment.
通过将125I标记的抗乙酰辅酶A羧化酶与大鼠肝脏多核糖体结合,已鉴定出参与乙酰辅酶A羧化酶[乙酰辅酶A:二氧化碳连接酶(ADP形成),EC 6.4.1.2]合成的特定多核糖体。这种结合具有高度特异性,并且是通过识别多核糖体上的新生肽链而发生的。利用125I标记抗体结合技术已证明,在不同饮食条件下的大鼠以及接受或未接受胰岛素治疗的四氧嘧啶糖尿病大鼠中,肝脏中合成乙酰辅酶A羧化酶的多核糖体的相对含量与该酶的肝脏合成速率密切相关。