Suppr超能文献

肌酸激酶脑同工酶。II. 酶的种属特异性以及兔和人横纹肌中无活性形式的存在

Brain isoenzyme of creatine kinase. II. Species specificity of enzyme and presence of inactive form in striated muscle of rabbit and man.

作者信息

Armstrong J B, Lowden J A, Sherwin A L

出版信息

J Biol Chem. 1977 May 25;252(10):3112-6.

PMID:863874
Abstract

Antibodies specific for the brain isoenzymes (BB) of creatine kinase were prepared by the injection of the highly purified rabbit enzyme into roosters. The antibodies were found to cross-react only partially with BB of rat, guinea pig, sheep, monkey, and man, demonstrating that these proteins are not entirely identical with respect to their antigenic sites. A greater degree of species specificity seems to exist for BB than for the muscle isoenzyme (MM) suggesting that BB may have undergone considerable evolutionary modification. Developmentally mature rabbit cardiac and skeletal muscles contained large quantites of an enzymatically inactive BB which can be detected immunochemically. It is antigenically identical with active rabbit BB but the two proteins can be separated by DEAE-cellulose chromatography. Enzymatically inactive BB is also present in human skeletal muscle. The presence of MM in muscle provides sufficient catalytic function and may have permitted the evolution of inactive BB in an additional (noncatalytic) metabolic role.

摘要

通过将高度纯化的兔肌酸激酶脑型同工酶(BB)注射到公鸡体内,制备了针对该同工酶的抗体。发现这些抗体仅与大鼠、豚鼠、绵羊、猴子和人类的BB发生部分交叉反应,表明这些蛋白质在抗原位点方面并不完全相同。与肌肉同工酶(MM)相比,BB似乎存在更高程度的物种特异性,这表明BB可能经历了相当大的进化修饰。发育成熟的兔心脏和骨骼肌含有大量酶活性无活性的BB,可通过免疫化学方法检测到。它在抗原性上与活性兔BB相同,但这两种蛋白质可通过DEAE-纤维素色谱法分离。酶活性无活性的BB也存在于人类骨骼肌中。肌肉中MM的存在提供了足够的催化功能,并且可能允许无活性BB在额外的(非催化)代谢作用中进化。

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