Evidence for albumin--cu(II)--amino acid ternary complex.
Evidence for albumin--cu(II)--amino acid ternary complex.
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白蛋白--cu(II)--氨基酸三元复合物的证据。
DOI：
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发表时间：
1968
期刊：
影响因子：
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通讯作者：
Y. Wigfield
中科院分区：
文献类型：
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作者：
B. Sarkar;Y. Wigfield
商业获得的纯人血清白蛋白（HSA）被证明含有分子聚集体，并显着污染Cu（II）。首先将商业HSA溶液通过Sephadex G-200柱以获得纯的单体HSA。随后使HSA的单体通过Chelex-100树脂以使其从Cu（II）中游离。所有Cu（II）结合研究均采用单体和无铜HSA进行。HSA上的第一个Cu（II）结合位点似乎比第二个和随后的结合位点更强。显着量的L-组氨酸和L-苏氨酸结合到HSA时，Cu（II）的形式加入Cu（II）-氨基酸络合物。在不存在Cu（II）的情况下，游离的L-组氨酸或L-苏氨酸在pH 7.4下不与HSA结合。它的结论是，在L-组氨酸或L-苏氨酸的存在下，三元复合物的形成涉及在第一和随后的结合位点的Cu（II）对HSA。鉴于这一发现，似乎HSA-Cu（II）和...
Commercially obtained pure human serum albumin (HSA) was shown to contain molecular aggregates and was significantly contaminated with Cu(II). A solution of commercial HSA was first passed through a Sephadex G-200 column to obtain pure monomeric HSA. The monomer of HSA was subsequently passed through Chelex-100 resin to free it from Cu(II). All Cu(II)-binding studies were conducted with monomeric and copper-free HSA. The first Cu(II)-binding site on HSA appears to be stronger than the second and the subsequent binding sites. Significant amounts of L-histidine and L-threonine were bound to HSA when Cu(II) was added in the form of Cu(II) – amino acid complexes. In the absence of Cu(II), free L-histidine or L-threonine do not bind to HSA at pH 7.4. It is concluded that, in the presence of either L-histidine or L-threonine, ternary complex formation is involved both at the first and the subsequent binding sites for Cu(II) on HSA. In view of this finding, it appears that the equilibrium between HSA–Cu(II) and ...