Shimomura O, Shimomura A
Biochem J. 1981 Dec 1;199(3):825-8. doi: 10.1042/bj1990825.
Although native aequorin is highly susceptible to inactivation, apoaequorin is highly resistant to various processes of denaturation. Apoaequorin was inactivated only partially at a temperature of 95 degrees C or by treatments with 6 M-urea, 4 M-guanidine hydrochloride, 1 M-HCl and 1 M-NaOH. It was nearly completely inactivated in 85% ethanol or by heating at 95 degrees C in 2 M-(NH4)2SO4, but over 50% of apoaequorin activity was restored in both cases merely by dissolving the coagulated protein in 4 M-guanidine hydrochloride. In the reconstitution of aequorin, partially inactivated apoaequorin yielded more aequorin than expected from the activity of the partially inactivated apoaequorin used, suggesting that the process of reconstitution promotes the renaturation of denatured apoaequorin.
尽管天然水母发光蛋白极易失活，但脱辅基水母发光蛋白对各种变性过程具有高度抗性。脱辅基水母发光蛋白仅在95℃的温度下或用6M尿素、4M盐酸胍、1M盐酸和1M氢氧化钠处理时才会部分失活。它在85%乙醇中几乎完全失活，或在2M硫酸铵中于95℃加热时也几乎完全失活，但在这两种情况下，仅通过将凝结的蛋白质溶解在4M盐酸胍中，就有超过50%的脱辅基水母发光蛋白活性得以恢复。在水母发光蛋白的重组过程中，部分失活的脱辅基水母发光蛋白产生的水母发光蛋白比根据所用部分失活脱辅基水母发光蛋白的活性预期的要多，这表明重组过程促进了变性脱辅基水母发光蛋白的复性。
