Fischer A C, Goode C A
Department of Chemistry and Biochemistry, California State University, Fullerton 92634.
Prep Biochem. 1994 May;24(2):151-65. doi: 10.1080/10826069408010089.
Binding of ceruloplasmin to bovine erythrocytes was investigated. The interaction was specific as demonstrated by more than 85% inhibition by excess ceruloplasmin protein. Binding was also inhibited by copper-nitrilotriacetate. The KD for both intact erythrocytes and solubilized ghost membranes was of the order of 10(-7) M. Using an affinity column a specific ceruloplasmin-binding protein was isolated from ghost membranes. The protein has an apparent molecular mass of 100,000 with subunits of 45 and 50 KDa.
对铜蓝蛋白与牛红细胞的结合进行了研究。这种相互作用具有特异性，过量的铜蓝蛋白可抑制85%以上的结合，这证明了其特异性。铜-次氮基三乙酸也可抑制结合。完整红细胞和溶解的血影膜的解离常数（KD）约为10^(-7) M。使用亲和柱从血影膜中分离出一种特异性铜蓝蛋白结合蛋白。该蛋白的表观分子量为100,000，亚基分子量分别为45 kDa和50 kDa。
