深红嗜盐菌L-丙氨酸脱氢酶的部分纯化及性质
Partial purification and properties of Halobacterium cutirubrum L-alanine dehydrogenase.
作者信息
Kim E K, Fitt P S
出版信息
Biochem J. 1977 Feb 1;161(2):313-20. doi: 10.1042/bj1610313.
Abstract
- Halobacterium cutirubrum L-alanine dehydrogenase was purified approx. 100-fold. 2. It has a mol. wt. of 72 500, about one-third that of two well-studied alanine dehydrogenases from non-halophiles. 3. The activity of the enzyme increases with temperature up to 70 degrees C, but the protein itself is not thermostable. 4. In the reductive amination reaction, the enzyme is fully active in the presence of high concentrations of K+, Na+ or NH4+ and partially active with Cs+ or Li+, but for oxidative deamination it has an absolute requirement for K+.
摘要
- 深红嗜盐菌L-丙氨酸脱氢酶被纯化了约100倍。2. 它的分子量为72500，约为两种已充分研究的非嗜盐菌丙氨酸脱氢酶分子量的三分之一。3. 该酶的活性随温度升高至70摄氏度而增加，但蛋白质本身不耐热。4. 在还原胺化反应中，该酶在高浓度的K⁺、Na⁺或NH₄⁺存在下完全有活性，在Cs⁺或Li⁺存在下部分有活性，但对于氧化脱氨反应，它绝对需要K⁺。
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