Teraoka H, Numa S
Eur J Biochem. 1975 May 6;53(2):465-70. doi: 10.1111/j.1432-1033.1975.tb04087.x.
Immunochemical techniques were used to study the mechanism underlying the marked increase in the level of acetyl-coenzyme A carboxylase activity in chick liver observed after hatching. The results of immunochemical titrations and Ouchterlony double-diffusion analysis indicated that this increase in the activity level of the enzyme was due to an elevation in the enzyme quantity. Isotopic leucine incorporation studies revealed that the rate of synthesis of the enzyme per liver was 18-fold higher in 9-day-old chicks than in 1-day-old chicks. In terms of the synthesis rate per gram of liver, this increase was 5-fold. The half-life for degradation of the enzyme in 9-day-old chicks was shown to be 46 h, whereas no apparent degradation of the enzyme as well as of total soluble liver protein was observed in 1-day-old chicks. These results indicate that the increase in the hepatic acetyl-CoA carboxylase content in growing chicks can be ascribed to accelerated synthesis of the enzyme.
采用免疫化学技术研究孵化后雏鸡肝脏中乙酰辅酶A羧化酶活性水平显著升高的潜在机制。免疫化学滴定和双向免疫扩散分析结果表明,该酶活性水平的升高是由于酶量的增加。同位素亮氨酸掺入研究显示,9日龄雏鸡肝脏中该酶的合成速率比1日龄雏鸡高18倍。以每克肝脏的合成速率计算,这种增加为5倍。结果表明,9日龄雏鸡中该酶降解的半衰期为46小时,而在1日龄雏鸡中未观察到该酶以及肝脏总可溶性蛋白有明显降解。这些结果表明,生长中雏鸡肝脏中乙酰辅酶A羧化酶含量的增加可归因于该酶合成的加速。