Suppr超能文献

人体组织及乳腺癌细胞中人类乙酰辅酶A羧化酶同工酶的鉴定

Identification of human acetyl-CoA carboxylase isozymes in tissue and in breast cancer cells.

作者信息

Witters L A, Widmer J, King A N, Fassihi K, Kuhajda F

机构信息

Department of Medicine, Dartmouth Medical School, Hanover, NH 03755-3833.

出版信息

Int J Biochem. 1994 Apr;26(4):589-94. doi: 10.1016/0020-711x(94)90018-3.

Abstract
  1. In the rat, acetyl-CoA carboxylase (ACC), a rate-limiting enzyme in fatty acid metabolism, exists as at least two different isozymes (M(r) 265,000 and 280,000) that display distinct tissue-specific distribution and regulation. 2. Based on the study of human tissue and human-derived breast cancer cell lines by enzyme isolation and protein blotting techniques, we have now identified two human isoforms of M(r) 265,000 (HACC 265) and 275,000 (HACC 275), each of which is homologous to one of the rat isozymes. 3. Human breast carcinoma cell lines show variable expression of these two isoforms, mirrored in the estimation of ACC acetyl-CoA kinetics.
摘要
  1. 在大鼠中,脂肪酸代谢的限速酶乙酰辅酶A羧化酶(ACC)至少以两种不同的同工酶形式存在(分子量分别为265,000和280,000),它们表现出不同的组织特异性分布和调控方式。2. 通过酶分离和蛋白质印迹技术对人体组织和人源乳腺癌细胞系进行研究后,我们现已鉴定出两种分子量分别为265,000(HACC 265)和275,000(HACC 275)的人同工型,它们各自与一种大鼠同工酶同源。3. 人乳腺癌细胞系显示出这两种同工型的可变表达,这在ACC乙酰辅酶A动力学估计中得到反映。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验