Bozzi M, Battistoni A, Sette M, Melino S, Rotilio G, Paci M
Department of Chemical Science and Technology, Tor Vergata University, Via della Ricerca Scientifica, 00133, Rome, Italy.
Int J Biol Macromol. 2001 Aug 20;29(2):99-105. doi: 10.1016/s0141-8130(01)00146-5.
The inactivation and the unfolding of the naturally monomeric Cu, Zn, superoxide dismutase from E. coli upon addition of sodium dodecylsulphate have been studied. In contrast to the bovine enzyme, CD, EPR, NMR spectroscopy and pulsed low resolution NMR measurements found an unfolding transition followed by inactivation of the enzyme. During this transition the active site becomes accessible to the bulk water. The unfolding is reversible and both, the tridimensional structure of the protein and the active site, can be restored upon dialysis. In addition, unfolding occurs without loss of metals in the solution.
研究了添加十二烷基硫酸钠后，来自大肠杆菌的天然单体铜锌超氧化物歧化酶的失活和去折叠情况。与牛酶不同，圆二色光谱（CD）、电子顺磁共振（EPR）、核磁共振（NMR）光谱以及脉冲低分辨率NMR测量发现，该酶先发生去折叠转变，随后失活。在这个转变过程中，活性位点变得可被大量水分子接近。去折叠是可逆的，通过透析可以恢复蛋白质的三维结构和活性位点。此外，去折叠过程中溶液中的金属不会丢失。
