Chang K, Williamson J R, Zarkowsky H S
J Clin Invest. 1979 Jul;64(1):326-8. doi: 10.1172/JCI109456.
Hereditary pyropikilocytosis is a hemolytic anemia in which the erythrocytes show increased sensitivity to heat-induced fragmentation. Circular dichroism measurements were employed to study the effect of heat on the secondary structure of pyropoikilocyte membrane proteins. The magnitude of the ellipticity at 222 nm over the temperature range from 25 degrees to 70 degrees C was determined for erythrocyte ghosts, spectrin, and ghost residue after extraction. In pyropoikilocyte ghosts, protein denaturation began at a lower temperature and the midpoint of the structural transition was displaced from 49 degrees C (the value for normal ghosts) to 44 degrees C. This thermal transition was present in spectrin, but not in the ghost residue after extraction. We conclude that an abnormality in the spectrin molecule alters the physical and morphologic properties of the erythrocyte membrane in pyropoikilocytosis.
遗传性热异形红细胞增多症是一种溶血性贫血，其中红细胞对热诱导的破碎表现出更高的敏感性。采用圆二色性测量来研究热对热异形红细胞膜蛋白二级结构的影响。测定了红细胞血影、血影蛋白和提取后的血影残余物在25℃至70℃温度范围内222nm处的椭圆率大小。在热异形红细胞血影中，蛋白质变性在较低温度下开始，结构转变的中点从49℃（正常血影的值）移至44℃。这种热转变存在于血影蛋白中，但不存在于提取后的血影残余物中。我们得出结论，血影蛋白分子的异常改变了热异形红细胞增多症中红细胞膜的物理和形态特性。
