Hoppe A, Theimer R R
Physiologische Chemie der Pflanzen, FB 9, Bergische Universität GH Wuppertal, Germany.
FEBS Lett. 1995 Oct 30;374(2):225-7. doi: 10.1016/0014-5793(95)01114-t.
A rapid and efficient method for the purification of malate synthase, an enzyme uniquely confined to glyoxysomes, from cotyledons of Brassica napus L. has been developed. The two step purification procedure is based on the consequent utilization of the tendency of malate synthase to form high molecular weight aggregates. Malate synthase was purified 75-fold to apparent homogeneity with a specific activity of 180 nkat/mg protein. The estimated molecular weight of malate synthase subunits was 63 kDa. Polyclonal antibodies raised against malate synthase in rabbits detect on Western blots only one single polypeptide with an identical molecular weight.
已开发出一种从甘蓝型油菜子叶中快速高效纯化苹果酸合酶的方法，苹果酸合酶是一种仅存在于乙醛酸循环体中的酶。两步纯化程序基于利用苹果酸合酶形成高分子量聚集体的趋势。苹果酸合酶纯化了75倍，达到表观均一性，比活性为180 nkat/mg蛋白质。苹果酸合酶亚基的估计分子量为63 kDa。用兔抗苹果酸合酶产生的多克隆抗体在蛋白质印迹上仅检测到一条分子量相同的单一多肽。
