Bidigare R R, Sander E G, Pettigrew D W
Biochim Biophys Acta. 1985 Sep 20;831(1):159-60. doi: 10.1016/0167-4838(85)90164-5.
Analytical gel permeation chromatography on both Sephadex and polyacrylamide columns shows that Clostridium oroticum dihydroorotase (L-5,6-dihydroorotate amidohydrolase, EC 3.5.2.3) undergoes a large decrease in molecular size when the pH is decreased from 8 to 6. The Stokes radius decreases from about 40 A to 36 A. Neither the molecular size nor kinetic properties are dependent on protein concentration. Thus, the decreased molecular size reflects a pH dependent isomerization of the enzyme.
在葡聚糖凝胶和聚丙烯酰胺柱上进行的分析性凝胶渗透色谱表明,当pH从8降至6时,乳清酸梭菌二氢乳清酸酶(L-5,6-二氢乳清酸酰胺水解酶,EC 3.5.2.3)的分子大小大幅减小。斯托克斯半径从约40埃降至36埃。分子大小和动力学性质均不依赖于蛋白质浓度。因此,分子大小的减小反映了该酶的pH依赖性异构化。