Suppr超能文献

一种用亮氨酸脱氢酶测定氨肽酶活性的分光光度法。

A spectrophotometric method for the determination of aminopeptidase activity with leucine dehydrogenase.

作者信息

Takamiya S, Ohshima T, Tanizawa K, Soda K

出版信息

Anal Biochem. 1983 Apr 1;130(1):266-70. doi: 10.1016/0003-2697(83)90678-4.

Abstract

L-Leucine dehydrogenase purified from Bacillus megaterium and Bacillus sphearicus was used for the determination of serum aminopeptidase activity with L-leucinamide as a substrate. L-Leucine produced by aminopeptidase was determined by measurement of the increase in absorbance at 340 nm caused by the formation of NADH. This method is useful for the kinetic studies of the aminopeptidase and the enzyme assay of a large number of samples. The serum aminopeptidase can be characterized to give some valuable information in clinical diagnosis by comparison of the results obtained by the present method with those by the conventional method with L-leucyl-p-nitroanilide as a substrate.

摘要

从巨大芽孢杆菌和球形芽孢杆菌中纯化得到的L-亮氨酸脱氢酶,以L-亮氨酰胺为底物用于测定血清氨肽酶活性。氨肽酶产生的L-亮氨酸通过测量由NADH形成引起的340nm处吸光度的增加来测定。该方法可用于氨肽酶的动力学研究以及大量样品的酶活性测定。通过将本方法所得结果与以L-亮氨酰对硝基苯胺为底物的传统方法所得结果进行比较,血清氨肽酶可得到表征,从而在临床诊断中提供一些有价值的信息。

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