Giroux E, Schoun J
J Inorg Biochem. 1981 Jul;14(4):359-62. doi: 10.1016/s0162-0134(00)80292-5.
An ultrafiltration technique was used to study stripping by glycine of the first copper and zinc ion equivalents bound by bovine, dog, and rat serum albumins at pH 7.5. Affinity of dog serum albumin for copper was poorer than for the other albumins, consistent with the absence in the former albumin of the copper binding site present at the amino terminus of the latter albumins. Affinities of all three proteins for zinc were similar, suggesting that the albumin amino terminus is not the primary zinc ion binding site.
采用超滤技术研究了在pH 7.5条件下，甘氨酸对牛、狗和大鼠血清白蛋白结合的首批铜离子和锌离子当量的剥离情况。狗血清白蛋白对铜的亲和力比其他白蛋白差，这与前者白蛋白中不存在后者白蛋白氨基末端的铜结合位点一致。所有三种蛋白质对锌的亲和力相似，表明白蛋白氨基末端不是主要的锌离子结合位点。
