Beltramini M, Santamaria M, Salvato B
Department of Biology, University of Padova, Italy.
Arch Biochem Biophys. 1988 Apr;262(1):149-58. doi: 10.1016/0003-9861(88)90177-4.
The reaction between Carcinus maenas hemocyanin and cyanide has been used for probing protein conformation in the presence of perturbants such as various anions, cations (Ca2+, Mg2+), and aliphatic alcohols. The kinetic parameters of the reaction are strongly affected by these agents, suggesting that the induced conformational modifications change the reactivity of the active site toward exogenous ligands. Different patterns are observed according to the perturbant used. As indicated by the mathematical treatment of the kinetic curves the affinity of the active site for CN- and O2 is affected much more than the rate constant of copper removal.
食蟹猴蛛血蓝蛋白与氰化物之间的反应已被用于在存在各种阴离子、阳离子（Ca2+、Mg2+）和脂肪醇等干扰剂的情况下探测蛋白质构象。这些试剂会强烈影响反应的动力学参数，这表明诱导的构象修饰改变了活性位点对外源配体的反应性。根据所使用的干扰剂观察到不同的模式。动力学曲线的数学处理表明，活性位点对CN-和O2的亲和力受影响程度远大于铜去除的速率常数。
