Redman C M, Marsh W L, Mueller K A, Avellino G P, Johnson C L
Transfusion. 1984 Mar-Apr;24(2):176-8. doi: 10.1046/j.1537-2995.1984.24284173356.x.
Kell blood-group-active protein has been isolated by labeling red cell surface proteins with 125I, sensitizing intact cells with anti-K1, anti-K2, anti-K7, or anti-K22, solubilizing the cell membranes, isolating immune complexes, and separating their components by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Each antibody separated a protein of approximately 93,000 daltons. Periodic-acid Schiff (PAS) staining of Kell protein showed that it was glycosylated. When separated under non-reducing conditions, Kell protein had different SDS-PAGE characteristics with protein bands of approximately 85,000 daltons and 115,000 daltons. This suggests that in the red cell membrane Kell protein is complexed with other proteins. Quantitative experiments made with anti-K7, anti-K22, and a mixture of anti-K7 and anti-K22 indicate that both antigen specificities are present in the same molecule. These biochemical data support serological studies which indicate that K22 is part of the Kell system.
通过用¹²⁵I标记红细胞表面蛋白、用抗K1、抗K2、抗K7或抗K22致敏完整细胞、溶解细胞膜、分离免疫复合物以及通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）分离其组分，已分离出凯尔血型活性蛋白。每种抗体都分离出一种分子量约为93,000道尔顿的蛋白质。凯尔蛋白的过碘酸希夫（PAS）染色显示它是糖基化的。在非还原条件下分离时，凯尔蛋白具有不同的SDS-PAGE特征，有分子量约为85,000道尔顿和115,000道尔顿的蛋白条带。这表明在红细胞膜中，凯尔蛋白与其他蛋白质复合。用抗K7、抗K22以及抗K7和抗K22的混合物进行的定量实验表明，两种抗原特异性存在于同一分子中。这些生化数据支持血清学研究，该研究表明K22是凯尔系统的一部分。
