Department of Biochemistry, University of Lund, Box 124, S-221 00, LUND, Sweden.
Photosynth Res. 1988 Jan;15(1):57-65. doi: 10.1007/BF00054988.
A rapid procedure for the purification of fructose-1,6-bisphosphate aldolase from spinach chloroplasts is presented which involves two steps; precipitation of bulk protein with polyethylene glycol and partitioning of remaining soluble protein in aqueous two-phase systems. A 94% pure preparation is obtained within 6h with a yield of 19%. A marked difference in the partition behaviour of the aldolase activity from whole leaf tissue suggested that the procedure is less efficient when leaf extract is used as starting material.
从菠菜叶绿体中快速纯化 1,6-二磷酸果糖醛缩酶的方法,该方法包括两个步骤:用聚乙二醇沉淀大量蛋白质和在双水相系统中分配剩余的可溶性蛋白质。在 6 小时内获得 94%纯度的酶制剂,产率为 19%。整个叶片组织中醛缩酶活性的分配行为存在明显差异,表明当使用叶提取物作为起始材料时,该方法效率较低。