Bamforth C W, Large P J
Biochem J. 1977 Nov 1;167(2):509-12. doi: 10.1042/bj1670509.
N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 unit/mg of protein, gave one band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, corresponding to a molecular weight of 130 000. Enzyme-Triton complexes were found to have a partial specific volume of 0.73 cm3/g, suggesting that the protein binds less than 0.1 g of Triton/g of protein. A molecular weight for the intact enzyme in the presence of 1% (w/v) Triton X-100 of 550 000 suggested that the enzyme may be a tetramer.
N-甲基谷氨酸脱氢酶纯化至比活性为0.29单位/毫克蛋白质，在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳上呈现一条带，对应分子量为130000。发现酶- Triton复合物的偏比容为0.73立方厘米/克，表明该蛋白质每克蛋白质结合的Triton少于0.1克。在1%（w/v）Triton X-100存在下，完整酶的分子量为550000，表明该酶可能是四聚体。
