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利用Ｓｏｕｔｈｗｅｓｔｅｒｎ印迹和电泳迁移率改变分析法，研究了处于终末分化阶段的人胚肝中、晚幼红细胞和经ｈｅｍｉｎ诱导分化前后的Ｋ５６２细胞核抽提物中与地高辛标记的ＨＳ２探针特异结合的蛋白质。发现经ｈｅｍｉｎ诱导后的Ｋ５６２细胞样品中出现一些为诱导前缺如的，分子量为１２，１４，１８，４５和５０ｋＤ的ＨＳ２结合蛋白。这些结合蛋白在印迹图谱中的位置（分子量大小）与存在于正常终末分化期红细胞中ＨＳ２结合蛋白的相近。同样，诱导后Ｋ５６２细胞核蛋白质与ＨＳ２形成复合物的电泳迁移图谱与正常分化的人胚肝红细胞核蛋白质－ＨＳ２复合物的相似，而与未经诱导的Ｋ５６２细胞核蛋白质－ＨＳ２复合物的迁移图谱存在差异。提示诱导分化和正常分化的红细胞表达一些新的ＨＳ２结合蛋白，这些仅在终末分化期红细胞中出现的ＨＳ２结合蛋白，可能是参与红细胞分化和珠蛋白基因表达调控的重要因素。
Southwestern blotting and electrophoretic mobility shift assay were used to study the specificity of digoxigenin-labeled HS2 probe in human embryonic liver at the terminal differentiation stage, late erythroblasts and K562 cell nuclear extracts before and after differentiation induced by hemin Binding protein. Some HS2-binding proteins with molecular weights of 12, 14, 18, 45 and 50 kD were found in K562 cells after induction of hemin. The location of these binding proteins in the blot (molecular size) is similar to that of HS2-binding proteins present in normal terminal differentiation erythrocytes. Similarly, the electrophoretic pattern of the complex formation of K562 cell nuclear proteins with HS2 after induction was similar to that of normal differentiated human embryonic liver erythrocyte nuclear protein-HS2 complex, but not with the un-induced nuclear protein-HS2 complex of K562 cells difference. These results suggest that differentiated and normal differentiated erythrocytes express some new HS2-binding proteins. These HS2-binding proteins, which appear only in the terminal differentiation erythrocytes, may be involved in the regulation of erythroid differentiation and globin gene expression.