Thornburgh B N, Wu L L, Griffin C C
Can J Biochem. 1978 Aug;56(8):836-8. doi: 10.1139/o78-127.
A procedure for the purification of Escherichia coli phosphofructokinase by affinity chromatography is described. The results of amino acid analyses of the purified protein and tryptic peptide mapping suggest that the tetrameric phosphofructokinase is composed of chemically identical subunits. In addition, the reaction product, ADP, was observed to bind to 4.1 +/- 0.1 equal and independent sites on the enzyme.
本文描述了一种通过亲和色谱法纯化大肠杆菌磷酸果糖激酶的方法。对纯化蛋白的氨基酸分析结果和胰蛋白酶肽图谱表明，四聚体磷酸果糖激酶由化学性质相同的亚基组成。此外，观察到反应产物ADP与该酶上4.1±0.1个等同且独立的位点结合。
