Amiconi G, Zolla L, Catanese B
Mol Cell Biochem. 1981 May 26;36(3):143-6. doi: 10.1007/BF02357030.
The oxygen equilibrium of human hemoglobin has been studied in the presence of 1-benzyl-3-indazoleoxyacetate (BZ). The results show that: (a) The overall oxygen affinity of hemoglobin is a function of BZ concentration, but the cooperative character of the equilibrium curve appears insensitive to the drug up to the maximal concentration studied (5 x 10(-2) M); (b) The functional expression of the interaction between hemoglobin and BZ is not affected by the presence of protons, i.e., the change in oxygen affinity determined by BZ is the same at any pH value studied; (c) The aromatic region of BZ molecules is of primary importance for the functional change of hemoglobin; (d) The difference in moles of BZ bound per mole of tetrameric unliganded and oxygenated hemoglobin corresponds to 2; these functionally relevant binding sites on the protein are probably located at alpha 1, beta 1 and alpha 2 beta 2 interfaces; (e) Thermodynamically, entropy effects dominate the reaction between hemoglobin and BZ.
在1-苄基-3-吲唑氧基乙酸酯（BZ）存在的情况下，对人血红蛋白的氧平衡进行了研究。结果表明：（a）血红蛋白的总体氧亲和力是BZ浓度的函数，但在研究的最大浓度（5×10⁻²M）之前，平衡曲线的协同特性似乎对该药物不敏感；（b）血红蛋白与BZ之间相互作用的功能表达不受质子存在的影响，即在任何研究的pH值下，由BZ决定的氧亲和力变化都是相同的；（c）BZ分子的芳香区域对血红蛋白的功能变化至关重要；（d）每摩尔四聚体未结合配体和氧合血红蛋白结合的BZ摩尔数差异为2；蛋白质上这些功能相关的结合位点可能位于α1、β1和α2β2界面；（e）从热力学角度来看，熵效应在血红蛋白与BZ的反应中占主导地位。
