Chaudhuri S, Coggins J R
Biochem J. 1985 Feb 15;226(1):217-23. doi: 10.1042/bj2260217.
A procedure was developed for the purification of shikimate dehydrogenase from Escherichia coli. Homogeneous enzyme with specific activity 1100 units/mg of protein was obtained in 21% overall yield. The subunit Mr estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 32 000. The native Mr, estimated by gel-permeation chromatography on a TSK G2000SW column, was also 32 000. E. coli shikimate dehydrogenase is therefore a monomeric NADP-linked dehydrogenase.
已开发出一种从大肠杆菌中纯化莽草酸脱氢酶的方法。以21%的总产率获得了比活性为1100单位/毫克蛋白质的纯酶。在十二烷基硫酸钠存在下通过聚丙烯酰胺凝胶电泳估计的亚基分子量为32000。通过在TSK G2000SW柱上进行凝胶渗透色谱法估计的天然分子量也为32000。因此，大肠杆菌莽草酸脱氢酶是一种单体的NADP连接脱氢酶。
