THE INTERACTION OF ZINC, NICKEL AND CADMIUM WITH SERUM-ALBUMIN AND HISTIDINE-RICH GLYCOPROTEIN ASSESSED BY EQUILIBRIUM DIALYSIS AND IMMUNOADSORBENT CHROMATOGRAPHY
THE INTERACTION OF ZINC, NICKEL AND CADMIUM WITH SERUM-ALBUMIN AND HISTIDINE-RICH GLYCOPROTEIN ASSESSED BY EQUILIBRIUM DIALYSIS AND IMMUNOADSORBENT CHROMATOGRAPHY
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DOI：
10.1016/0003-9861(82)90350-2
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发表时间：
1982-01-01
影响因子：
3.9
通讯作者：
MORGAN, WT
中科院分区：
文献类型：
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作者：
GUTHANS, SL;MORGAN, WT
人血清白蛋白(HSA)结合2-3mol Zn2+、Ni2+或Cd2+/mol蛋白质，表观Kd在10μM范围内。兔富含组氨酸的糖蛋白(HRG)分别结合13、9和6mol Zn2+、Ni2+和Cd2+/mol蛋白，具有表观Kd约。 10微米HRG 与金属的结合表现出正协同性，因此表观 Kd 可能低估了 HRG 对金属离子的真实亲和力。 HSA和HRG对金属离子的相对亲和力为Zn2+>Ni2+>Cd2+。 His（一种血清金属螯合剂）影响两种蛋白质与 Ni2+ 的结合，但不影响 Zn2+ 或 Cd2+ 的结合。在HSA(250μM)、HRG(2.5μM)和His(100μM)的生理浓度下，HRG以25μM的总金属浓度结合36％的Zn2+、9％的Ni2+和13％的Cd2+。在相同条件下，HSA 含有 37% 的 Zn2+、14% 的 Ni2+ 和 56% 的 Cd2+。 HSA 对 3 种金属的内在亲和力比 HRG 低，但预计会与血清中更高比例的这些金属结合。制备了特异性免疫吸附柱，用于直接研究血清中HRG对金属的结合。与相应金属离子孵育后，65Zn2+ 和 63Ni2+ 与等份兔血清中的 HRG 相关。 HRG 是血清中的金属结合成分。
Human serum albumin (HSA) bound 2-3 mol Zn2+, Ni2+ or Cd2+/mol protein with apparent Kd in the range of 10 .mu.M. Rabbit His-rich glycoprotein (HRG) bound 13, 9 and 6 mol Zn2+, Ni2+ and Cd2+/mol protein, respectively, with apparent Kd .apprx. 10 .mu.M. The binding of metals by HRG exhibited positive cooperativity, so that the apparent Kd may have underestimated HRG true affinity for metal ions. The relative affinities of HSA and HRG for metal ions were Zn2+ > Ni2+ > Cd2+. His (a serum metal chelator) affected the binding of Ni2+ by both proteins but not that of Zn2+ or Cd2+. At physiological concentrations of HSA (250 .mu.M), HRG (2.5 .mu.M) and His (100 .mu.M), HRG bound 36% of the Zn2+, 9% of the Ni2+ and 13% of the Cd2+ at a total metal concentration of 25 .mu.M. Under the same conditions HSA held 37% of the Zn2+, 14% of the Ni2+ and 56% of the Cd2+. HSA had a lower intrinsic affinity for the 3 metals than HRG but would be expected to bind a higher proportion of these metals in serum. A specific immunoadsorbent column was prepared and used to study the metal binding by HRG in serum directly. 65Zn2+ and 63Ni2+ were associated with HRG in aliquots of rabbit serum after incubation with the corresponding metal ion. HRG was a metal binding component of serum.