Shaklai N, Ranney H R
Isr J Med Sci. 1978 Nov;14(11):1152-6.
The binding of hemoglobin to phosphatidylserine liposomes was studied by Hb quenching of the fluorescence intensity of 12-(9-anthroyl) stearic acid embedded in the lipid membrane. The interaction is basically electrostatic. Hb A2 interacts more strongly than Hb A. The binding always includes an irreversible fraction. Interaction of Hb with normal red blood cell membranes was studied with the same technique. The main difference between the two systems is that the binding of Hb to the inner surface of the red cell membrane is based on the interaction of Hb with the membrane proteins and is reversible. The inner side of the red blood cell membrane is composed of phosphatidylserine lipids but these are normally masked by membrane proteins. In cases where Hb A2 is higher or when membrane lipids are abnormally exposed, Hb might interact irreversibly with the lipid layer and distort the membrane.
通过脂质膜中嵌入的12 -（9 - 蒽酰基）硬脂酸荧光强度的血红蛋白淬灭来研究血红蛋白与磷脂酰丝氨酸脂质体的结合。这种相互作用基本上是静电作用。Hb A2的相互作用比Hb A更强。这种结合总是包含一个不可逆的部分。用相同技术研究了血红蛋白与正常红细胞膜的相互作用。这两个系统的主要区别在于，血红蛋白与红细胞膜内表面的结合基于血红蛋白与膜蛋白的相互作用，并且是可逆的。红细胞膜的内侧由磷脂酰丝氨酸脂质组成，但这些通常被膜蛋白掩盖。在Hb A2较高或膜脂质异常暴露的情况下，血红蛋白可能与脂质层发生不可逆相互作用并使膜变形。
