Ribarov S R, Benchev I C, Strashimirov D D
Biochem J. 1984 Apr 1;219(1):317-20. doi: 10.1042/bj2190317.
Methaemoglobin may be an important factor for initiation and development of lipid peroxidation in Cu(II)-treated red blood cells. It seems likely that the initiation of peroxidation by methaemoglobin is only possible if direct contact between haemoglobin molecule and the cell membrane is realized. In view of this, the binding of haemoglobin to the red-blood-cell membrane in the presence of CuCl2 was studied. It was found that the haemoglobin quenching of the fluorescence of 12-(9-anthroyl)stearic acid-labelled red-blood-cell membranes greatly increases in the presence of CuCl2. This effect is relatively independent of pH and the ionic strength of the medium, indicating that in this case the binding of haemoglobin is not electrostatic in nature. The haemoglobin quenching of the fluorescence of the inside-out and the right-side-out resealed ghosts were almost the same in the presence of CuCl2. This result suggests that, in the presence of ionic copper, both surfaces of the membrane possess approximately equal amounts of sites for the binding of haemoglobin.
高铁血红蛋白可能是铜（II）处理的红细胞中脂质过氧化起始和发展的一个重要因素。高铁血红蛋白引发过氧化作用似乎只有在血红蛋白分子与细胞膜实现直接接触时才有可能。鉴于此，研究了在氯化铜存在的情况下血红蛋白与红细胞膜的结合情况。研究发现，在氯化铜存在的情况下，12-（9-蒽甲酰基）硬脂酸标记的红细胞膜荧光的血红蛋白猝灭作用大大增强。这种效应相对独立于pH值和介质的离子强度，表明在这种情况下血红蛋白的结合本质上不是静电作用。在氯化铜存在的情况下，内翻和外翻重封膜泡的荧光的血红蛋白猝灭作用几乎相同。这一结果表明，在离子铜存在的情况下，膜的两个表面具有大致等量的血红蛋白结合位点。
