Chaudhuri S, Lambert J M, McColl L A, Coggins J R
Biochem J. 1986 Nov 1;239(3):699-704. doi: 10.1042/bj2390699.
A procedure has been developed for the purification of 3-dehydroquinase from Escherichia coli. Homogeneous enzyme with specific activity 163 units/mg of protein was obtained in 19% overall yield. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate was 29,000. The native Mr, estimated by gel permeation chromatography on Sephacryl S-200 (superfine) and on TSK G3000SW, was in the range 52,000-58,000, indicating that the enzyme is dimeric. The catalytic properties of the enzyme have been determined and shown to be very similar to those of the biosynthetic 3-dehydroquinase component of the arom multifunctional enzyme of Neurospora crassa.
已开发出一种从大肠杆菌中纯化3-脱氢奎尼酸酶的方法。获得了比活性为163单位/毫克蛋白质的纯酶，总产率为19%。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29,000。通过在Sephacryl S - 200（超细）和TSK G3000SW上进行凝胶渗透色谱法估计的天然分子量在52,000 - 58,000范围内，表明该酶是二聚体。已确定该酶的催化特性，并且显示其与粗糙脉孢菌芳香族多功能酶的生物合成3-脱氢奎尼酸酶组分的催化特性非常相似。
