Wallach D F, Schmidt-Ullrich R
J Cell Physiol. 1976 Dec;89(4):771-4. doi: 10.1002/jcp.1040890441.
Binding of concanavalin A to isolated thymocyte membrane vesicles occurs through (a) numerous (approximately 6 x 106/cell equivalent) low-affinity sites (Ka = 1.3 x 105M-1) anf (b) fewer (approximately 0.4 x 106/cell equipment) specific receptors (Ka = 6.8 x 106 M-1) defined as 55,000 D glycoprotein and its multimers. Specific binding is positively-cooperative, with a Hill coefficient of approximately 1.8. Low concentrations of glutaraldehyde selectively crosslink the 55,000 D glycoprotein with replacement of positively-cooperative sites by high-affinity sites. It is proposed that concavalin A-binding induces multimerization of the 55,000 D glycoprotein.
伴刀豆球蛋白A与分离的胸腺细胞膜囊泡的结合通过以下两种方式发生：（a）众多（约6×10⁶/细胞当量）低亲和力位点（Ka = 1.3×10⁵M⁻¹）；（b）较少（约0.4×10⁶/细胞当量）的特异性受体（Ka = 6.8×10⁶M⁻¹），这些受体被定义为55,000 D糖蛋白及其多聚体。特异性结合是正协同的，希尔系数约为1.8。低浓度的戊二醛选择性地交联55,000 D糖蛋白，使正协同位点被高亲和力位点取代。有人提出，伴刀豆球蛋白A结合诱导55,000 D糖蛋白多聚化。
