Kinetic studies of yeast hexokinase.
Kinetic studies of yeast hexokinase.
复制标题
酵母己糖激酶的动力学研究。
DOI：
10.1016/s0021-9258(18)50115-0
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发表时间：
1962
期刊：
影响因子：
--
通讯作者：
V. Zewe
中科院分区：
文献类型：
--
作者：
H. Fromm;V. Zewe
结果初始反应速度测量图1和图2显示了用酵母己糖激酶获得的数据的Lineweaver-Burk图(12)。定性上，Reynard等人(13)和Frieden(14)在丙酮酸激酶和Frieden(14)中得到了非常相似的结果，根据Kornberg(10)，添加了一定量的葡萄糖6-磷酸脱氢酶，可以催化每分钟7Xlop6M TPN的还原。在这些研究中使用的最高底物浓度下，己糖激酶每分钟允许大约2×10-6M TPN减少。2重复图1和图2的数据，ME+：ATP2.0：1，2.5：1，3.0：1，3.5：L，镁离子与三磷酸腺苷的比例为2.5：1，3.5：1，无明显抑制作用。激活。三磷酸腺苷和葡萄糖米氏常数的变化。或
RESULTSInitial Reaction Velocity Measurements-h Figs. 1 and 2 are shown Lineweaver-Burk plots (12) of data obtained with yeast hexokinase. Qualitatively, very similar results have been obtained by Reynard et al.(13) with pyruvate kinase and by Frieden (14) with diphosphopyridine nucleotide-cytochrome c re-1 An amount of glucose 6-phosphate dehydrogenase was added that could catalyze the reduction of 7 X lop6 M TPN per minute according to Kornberg(10). At the highest substrate concentrations used in these studies, hexokinase permitted approximately 2 X lop6 M TPN reduction per minute. 2 The data of Figs. 1 and 2 were repeated at ME++ to ATP ratios of 2.0: 1, 2.5: 1, 3.0: 1, and 3.5: l. Between Mg++-to ATP ratios of 2.5: 1 and 3.5: 1, there was no evidence of inhibition. activation. alteration of the Michaelis constants of ATP and glucose. or