Amiot M, Bernard A, Tran H C, Leca G, Kanellopoulos J M, Boumsell L
Scand J Immunol. 1986 Jan;23(1):109-18. doi: 10.1111/j.1365-3083.1986.tb01948.x.
Monoclonal antibody K20 recognizes a human glycoprotein complex that is not restricted to haematopoietic lineages but is preferentially expressed on early haematopoietic cells, T cells, and monocytes. This glycoprotein complex is made of a constant 120,000-140,000 Mr subunit noncovalently associated at the cell surface with subunits of higher Mr ranging from 150,000 to 200,000 on different cell types. Internal labelling with [35S]methionine and pulse-chase experiments revealed that in the cell the 120,000 Mr glycoprotein of this complex is also noncovalently associated with a 100,000 Mr glycoprotein, and that both glycoproteins are independently biosynthesized. This glycoprotein complex is shown by immunoprecipitation by lectin plus antilectin antibodies and by sequential immunoprecipitations to be one of the cell surface structures bound by phytohaemagglutinin on the surface of normal T cells.
单克隆抗体K20识别一种人类糖蛋白复合物,该复合物不限于造血谱系,而是优先在早期造血细胞、T细胞和单核细胞上表达。这种糖蛋白复合物由一个恒定的120,000 - 140,000 Mr亚基组成,在细胞表面与不同细胞类型上Mr范围为150,000至200,000的较高Mr亚基非共价结合。用[35S]甲硫氨酸进行内部标记和脉冲追踪实验表明,在细胞中,该复合物的120,000 Mr糖蛋白也与100,000 Mr糖蛋白非共价结合,并且这两种糖蛋白都是独立生物合成的。通过凝集素加抗凝集素抗体的免疫沉淀以及连续免疫沉淀表明,这种糖蛋白复合物是正常T细胞表面被植物血凝素结合的细胞表面结构之一。