Anstee D J
Blood Group Reference Laboratory, South Western Regional Blood Transfusion Centre, Southmead, Bristol, UK.
Vox Sang. 1990;58(1):1-20. doi: 10.1111/j.1423-0410.1990.tb02049.x.
The surface of the human red blood cell is dominated by a small number of abundant blood group active proteins. The major proteins are the anion transport protein (band 3) which has AB(H) activity, and Glycophorin A which has MN activity. Band 3 and Glycophorin A are of equal abundance in the normal red cell membrane (approximately 10(6) copies of each) and the two proteins may associate together as a complex. The glucose transporter (band 4.5) had AB(H) activity and there are about 5 x 10(5) copies/red cell. Several polypeptides associate together to form the Rh complex. The major components of this complex (abundance 1-2 x 10(5) copies/red cell) are polypeptides of Mr 30,000, polypeptides of Mr 45,000-100,000 and Glycophorin B. The antigens of the Rh blood group system appear to be associated with the polypeptides of Mr 30,000 and those of Mr 45,000-100,000 (the latter also express AB(H) activity). Glycophorin B expresses the blood group 'N' antigen and the Ss antigens. Glycophorins C and D carry the Gerbich antigens and, together, these polypeptides comprise approximately 10(5) copies/red cell. The complete protein sequence of all the above-mentioned proteins is known, except for the Mr 30,000 and Mr 45,000-100,000 polypeptides of the Rh complex for which only partial sequences are available, and Glycophorin D, the sequence of which can be inferred from that of Glycophorin C. Several of the minor blood group active proteins at the red cell surface (abundance less than 1.2 x 10(4)/red cell) have been the subject of recent studies. The polypeptide expressing Cromer-related blood group antigens has been identified as decay-accelerating factor and that carrying the Ina/Inb antigens as CD44. The protein sequence of both of these proteins has been deduced form nucleotide sequencing. The polypeptides expressing Kell antigens, Lutheran antigens, Fy antigens, and LW antigens have also been identified and partially characterised.
人类红细胞表面由少数几种丰富的血型活性蛋白主导。主要蛋白是具有AB(H)活性的阴离子转运蛋白（带3蛋白）和具有MN活性的血型糖蛋白A。在正常红细胞膜中，带3蛋白和血型糖蛋白A的丰度相等（每种约10^6个拷贝），这两种蛋白可能作为复合物结合在一起。葡萄糖转运蛋白（带4.5蛋白）具有AB(H)活性，每个红细胞约有5×10^5个拷贝。几种多肽结合在一起形成Rh复合物。该复合物的主要成分（丰度为1 - 2×10^5个拷贝/红细胞）是分子量为30,000的多肽、分子量为45,000 - 100,000的多肽和血型糖蛋白B。Rh血型系统的抗原似乎与分子量为30,000的多肽以及分子量为45,000 - 100,000的多肽相关（后者也表达AB(H)活性）。血型糖蛋白B表达血型“N”抗原和Ss抗原。血型糖蛋白C和D携带Gerbich抗原，这些多肽加起来每个红细胞约有10^5个拷贝。除了Rh复合物中分子量为30,000和分子量为45,000 - 100,000的多肽（仅有部分序列可用）以及血型糖蛋白D（其序列可从血型糖蛋白C的序列推断得出）外，上述所有蛋白的完整蛋白质序列均已明确。红细胞表面几种次要的血型活性蛋白（丰度小于1.2×10^4/红细胞）是近期研究的对象。表达与克罗马血型相关抗原的多肽已被鉴定为衰变加速因子，携带Ina/Inb抗原的多肽被鉴定为CD44。这两种蛋白的蛋白质序列均已通过核苷酸测序推导得出。表达Kell抗原、路德抗原、Fy抗原和LW抗原的多肽也已被鉴定并部分表征。
