Albery W J, Knowles J R
Biochemistry. 1976 Dec 14;15(25):5627-31. doi: 10.1021/bi00670a031.
The experimental results on the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate catalyzed by triosephosphate isomerase that are presented in the previous five papers are here collected and analyzed according to the theory presented in the first paper (Albery, W.J., Knowles, J.R. (1976), Biochemistry 15, the first of eight papers in a series in this issue). The rate constants and fractionation factors so derived allow the construction of theGibbs free-energy profile for this enzyme-catalyzed reaction.
前三篇论文中所展示的关于磷酸丙糖异构酶催化磷酸二羟丙酮和3-磷酸-D-甘油醛相互转化的实验结果，在这里根据第一篇论文（阿尔伯里，W.J.，诺尔斯，J.R.（1976年），《生物化学》15卷，本期系列八篇论文中的第一篇）中提出的理论进行了收集和分析。由此得出的速率常数和分馏系数可用于构建该酶催化反应的吉布斯自由能分布图。
