Suppr超能文献

影响大肠杆菌K12中L-丝氨酸脱氨酶活性体内稳定性的因素。

Factors influencing the in vivo stability of L-serine deaminase activity in E. coli K12.

作者信息

Beeraj R D, Morris J F, Newman E B

出版信息

Can J Microbiol. 1978 Dec;24(12):1607-13. doi: 10.1139/m78-257.

Abstract

L-Serine deaminase (L-SD) is unstable in intact cells of Escherichia coli K12. The extent of this instability is dependent on the nitrogen content of the medium in which the enzyme is synthesized, and on that in which it is tested. Enzyme activity in cells grown with an inorganic nitrogen source is unstable in the presence of inorganic nitrogen; enzyme activity in cells grown with an organic nitrogen source is unstable in the presence of the amino acids glycine and leucine.

摘要

L-丝氨酸脱氨酶(L-SD)在大肠杆菌K12的完整细胞中不稳定。这种不稳定性的程度取决于合成该酶的培养基中的氮含量,以及测试该酶时培养基中的氮含量。用无机氮源培养的细胞中的酶活性在无机氮存在下不稳定;用有机氮源培养的细胞中的酶活性在甘氨酸和亮氨酸存在下不稳定。

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