Sutherland R, Delia D, Schneider C, Newman R, Kemshead J, Greaves M
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4515-9. doi: 10.1073/pnas.78.7.4515.
A murine monoclonal antibody (OKT9) raised against human leukemic cells binds to a wide variety of leukemia and tumor cell lines and to a minority of leukemia cells taken directly from patients. Fetal thymus and liver are strongly reactive as are some normal, immature hemopoietic cells and activated lymphocytes. Reactivity with OKT9 appears to correlate with proliferation status in both normal and malignant populations. Biochemical analysis indicates that this structure is a approximately equal to 180,000-dalton glycoprotein with two disulfide-bonded subunits of approximately equal to 90,000-daltons. Isolation of the transferrin receptor from a T-cell line (MOLT-4) indicates that it also has a dimeric approximately equal to 180,000-dalton structure. Radio-labeled transferrin bound to its receptors can be specifically precipitated by the monoclonal OKT9, although the latter does not bind transferrin itself, indicating that the antigenic structure defined by this antibody is likely to be the transferrin receptor.
一种针对人类白血病细胞产生的鼠单克隆抗体（OKT9）可与多种白血病和肿瘤细胞系结合，也能与直接取自患者的少数白血病细胞结合。胎儿胸腺和肝脏有强烈反应，一些正常的未成熟造血细胞和活化淋巴细胞也有反应。OKT9的反应性似乎与正常和恶性细胞群体中的增殖状态相关。生化分析表明，这种结构是一种约180,000道尔顿的糖蛋白，由两个约90,000道尔顿的二硫键连接亚基组成。从T细胞系（MOLT-4）中分离出的转铁蛋白受体也具有约180,000道尔顿的二聚体结构。与受体结合的放射性标记转铁蛋白可被单克隆OKT9特异性沉淀，尽管后者本身不结合转铁蛋白，这表明该抗体所定义的抗原结构可能就是转铁蛋白受体。
