Haralambie G
Enzyme. 1977;22(5):330-5. doi: 10.1159/000458813.
Citrate synthase activity in soluble human muscle extracts (KCl-containing triethanolamine buffer) amounts to 17.5+/-6.97 U/g wet weight at 37 degrees C (n=36 healthy male subjects). Double determinations, both using two procedures and with muscle samples divided into two pieces and analyzed separately, gave very good reproducibilities. The possible causes of the comparatively high values are discussed. Significant correlations of citrate synthase activity with NADP-linked isocitrate dehydrogenase (r=+0.826) and hexose phosphate isomerase (r=-0.582) were found. The distribution of citrate synthase activity in the samples studied is not of the normal type but appears to be binomial.
在37摄氏度下，可溶性人体肌肉提取物（含氯化钾的三乙醇胺缓冲液）中的柠檬酸合酶活性为17.5±6.97 U/g湿重（n = 36名健康男性受试者）。采用两种方法并将肌肉样本分成两块分别进行分析的双份测定，具有非常好的重复性。文中讨论了这些相对较高数值的可能原因。发现柠檬酸合酶活性与NADP连接的异柠檬酸脱氢酶（r = +0.826）和磷酸己糖异构酶（r = -0.582）存在显著相关性。所研究样本中柠檬酸合酶活性的分布并非正态分布，而是呈二项分布。
