Lewis J G, André C M
Immunol Commun. 1981;10(6):541-7. doi: 10.3109/08820138109055704.
The binding of 125I-alpha 2HS glycoprotein to peripheral blood monocytes was investigated at 4 degrees C. Equilibrium was attained after 60 min incubation with little internalization of radiolabeled protein. Binding was partially dependent on Ca++. Scatchard plot analysis revealed a dissociation constant of 10(-4) M with 10(6) sites/cell. The low binding affinity between alpha 2HS glycoprotein and peripheral blood monocytes may be offset by the relatively high serum concentration of this protein in the expression of its phagocytic enhancing properties.
在4℃下研究了125I-α2HS糖蛋白与外周血单核细胞的结合。孵育60分钟后达到平衡,放射性标记蛋白很少内化。结合部分依赖于Ca++。Scatchard图分析显示解离常数为10^(-4)M,每个细胞有10^6个位点。α2HS糖蛋白与外周血单核细胞之间较低的结合亲和力可能会被该蛋白相对较高的血清浓度所抵消,从而发挥其吞噬增强特性。