Cerdonio M, Morante S, Vitale S, De Young A, Noble R W
Proc Natl Acad Sci U S A. 1980 Mar;77(3):1462-5. doi: 10.1073/pnas.77.3.1462.
Deionized carp carbon monoxide hemoglobin in distilled water or in bis(2-hydroxyethyl)imino-tris(hydroxymethyl)methane or Tris buffer exhibits a slight but significant paramagnetism. This is most clearly demonstrated by the decrease in this paramagnetism that is caused by the addition of inositol hexaphosphate to this protein in the former buffer at pH 6.3-6.4. No such effect is seen when inositol hexaphosphate is added to carp cyanomethemoglobin, demonstrating that the change observed with carbon monoxide derivative is not due to a modification in the diamagnetic properties of the protein.
去离子鲤鱼一氧化碳血红蛋白在蒸馏水、双(2-羟乙基)亚氨基三(羟甲基)甲烷或Tris缓冲液中呈现出轻微但显著的顺磁性。在pH 6.3 - 6.4的前一种缓冲液中,向该蛋白质添加肌醇六磷酸会导致顺磁性降低,这最清楚地证明了这一点。当向鲤鱼氰化高铁血红蛋白中添加肌醇六磷酸时,未观察到这种效应,这表明一氧化碳衍生物所观察到的变化并非由于蛋白质抗磁性性质的改变。