Nissler K, Schellenberger W, Hofmann E
Acta Biol Med Ger. 1977;36(7-8):1027-33.
Binding of MgATP to yeast phosphofructokinase was investigated by the gel filtration equilibrium dialysis technique. Per subunit of yeast phosphofructokinase two molecules of MgATP are bound in the absence of fructose-6-phosphate, one to a high-affinity and one to a low-affinity site. The experimental data were compared with a kinetic model of yeast phosphofructokinase as described by Freyer et al. [3].
采用凝胶过滤平衡透析技术研究了MgATP与酵母磷酸果糖激酶的结合。在不存在6-磷酸果糖的情况下，酵母磷酸果糖激酶每个亚基结合两分子MgATP，一个结合到高亲和力位点，一个结合到低亲和力位点。将实验数据与Freyer等人[3]描述的酵母磷酸果糖激酶动力学模型进行了比较。
