Takamiya S, Ohshima T, Tanizawa K, Soda K
Anal Biochem. 1983 Apr 1;130(1):266-70. doi: 10.1016/0003-2697(83)90678-4.
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.
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。
