Binding and uptake of copper from ceruloplasmin.
Binding and uptake of copper from ceruloplasmin.
复制标题
从铜蓝蛋白中结合和摄取铜。
DOI：
10.1016/s0006-291x(86)80064-x
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发表时间：
1986
影响因子：
3.1
通讯作者：
Linder,MC
中科院分区：
文献类型：
--
作者：
Orena,SJ;Goode,CA;Linder,MC
[67铜]血浆铜蓝蛋白的特异性结合，含有从大鼠组织制备的质膜显示在存在过量的非放射性铜（II）或血浆铜蓝蛋白。与Cu（II）有正协同作用，表观KD为10− 7 M。两种“冷”配体的影响在一定程度上是相加的。没有“特异性”结合显示与锌（II），无关的蛋白质和煮沸后的膜。[67 Cu]铜蓝蛋白的总结合率和特异性结合率在心脏和大脑中比在肝脏中高2-7倍，每g组织或每mg蛋白，±校正5′-核苷酸酶的产率。Cu（II）也抑制CHO细胞从血浆铜蓝蛋白中摄取[67 Cu]，但莫能菌素没有，这表明血浆铜蓝蛋白Cu的摄取发生在细胞表面。
Specific binding of [67Cu]ceruloplasmin to plasma membrane containing preparations from rat tissues was shown in the presence of an excess of non-radioactive Cu(II) or ceruloplasmin. With Cu(II) there was positive cooperativity and an apparent KDof 10−7M. 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.