猪肌肉提取物中的亮氨酸氨肽酶。
Leucine aminopeptidase in extracts of swine muscle.
作者信息
Joseph R L, Sanders W J
出版信息
Biochem J. 1966 Sep;100(3):827-32. doi: 10.1042/bj1000827.
Abstract
- Leucine aminopeptidase (EC 3.4.1.1) has been demonstrated in swine muscle at a level of activity one-fifth that of the swine kidney. 2. The enzyme has been purified 110-fold by precipitation with ammonium sulphate, heat treatment and chromatography on Sephadex G-100. 3. The enzyme is heat-stable, but is rapidly inactivated below pH7. It requires Mg(2+) or Mn(2+) for activity. The Michaelis constant for leucine amide with Mg(2+)-activated enzyme is 5.0x10(-3)m. 4. Muscle leucine aminopeptidase is very similar to the kidney enzyme.
摘要
- 亮氨酸氨肽酶（EC 3.4.1.1）已在猪肌肉中得到证实，其活性水平是猪肾脏的五分之一。2. 通过硫酸铵沉淀、热处理以及在葡聚糖凝胶G - 100上进行色谱分离，该酶已被纯化了110倍。3. 该酶对热稳定，但在pH7以下会迅速失活。其活性需要Mg(2+)或Mn(2+)。Mg(2+)激活的酶对亮氨酰胺的米氏常数为5.0×10(-3)m。4. 肌肉中的亮氨酸氨肽酶与肾脏中的酶非常相似。
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