Orena S J, Goode C A, Linder M C
Biochem Biophys Res Commun. 1986 Sep 14;139(2):822-9. doi: 10.1016/s0006-291x(86)80064-x.
Specific binding of [67Cu]ceruloplasmin to plasma membrane containing preparations from rat tissues was shown in the presence of an excess of nonradioactive Cu(II) or ceruloplasmin. With Cu(II) there was positive cooperativity and an apparent KD of 10(-7) M. The effects of both "cold" ligands was partly additive. No "specific" binding was shown with Zn(II), unrelated proteins and after boiling the membranes. Total and specific binding of [67Cu]ceruloplasmin were 2-7 fold greater for heart and brain than for liver preparations, per g tissue or per mg protein, +/- correction for yield of 5'-nucleotidase. Cu(II) also inhibited uptake of [67Cu] from ceruloplasmin by CHO cells, but monensin did not, suggesting uptake of ceruloplasmin Cu occurs at the cell surface.
在存在过量非放射性铜（II）或铜蓝蛋白的情况下，显示出[67Cu]铜蓝蛋白与来自大鼠组织的含质膜制剂有特异性结合。对于铜（II），存在正协同性，表观解离常数为10^(-7) M。两种“冷”配体的作用部分是相加的。对于锌（II）、无关蛋白质以及膜煮沸后，未显示出“特异性”结合。每克组织或每毫克蛋白质计算，[67Cu]铜蓝蛋白在心脏和脑组织中的总结合和特异性结合比肝脏制剂大2至7倍，±对5'-核苷酸酶产率的校正。铜（II）也抑制CHO细胞从铜蓝蛋白摄取[67Cu]，但莫能菌素没有，这表明铜蓝蛋白铜的摄取发生在细胞表面。
