Tinteris L V, Shaposhnikov A M
Biokhimiia. 1978 Jun;43(6):979-87.
Study of the interactions of homogenous human ceruloplasmin preparations with histamine show that the rate of p-phenylene diamine oxidation by ceruloplasmin is increased in the presence of histamine; the increase in the enzyme activity is independent of histamine concentration. The dependence of the reaction rate on substrate concentration is S-shaped, both in the presence and in the absence of histamine. The respective values of the Hill coefficient and Rs for the enzyme in the presence and in the absence of histamine are 2.5 and 2.0 and 8.0 and 10.4. Histamine does not change ceruloplasmin-specific absorption at 610 nm. Evidence from EPR studies show that histamine does not interact with Cu of the enzyme active center. During interaction with histamine the antigenic properties of the enzyme are changed. Histamine increases the oxidase activity of the enzyme in human and rat blood sera and exerts multifold effects on the enzyme activity in patients with hepatolenticular degeneration. After injection of histamine to rats the enzyme activity is increased without a simultaneous increase in Cu concentration in the blood serum, i.e. without de novo synthesis of ceruloplasmin. The data obtained suggest that ceruloplasmin is probably an allosteric enzyme, which histamine is its positive allosteric effector.
对人源同质性铜蓝蛋白制剂与组胺相互作用的研究表明，在组胺存在的情况下，铜蓝蛋白氧化对苯二胺的速率会增加；酶活性的增加与组胺浓度无关。无论有无组胺存在，反应速率对底物浓度的依赖性均呈S形。有组胺和无组胺时该酶的希尔系数（Hill coefficient）和Rs值分别为2.5和2.0以及8.0和10.4。组胺不会改变铜蓝蛋白在610 nm处的特异性吸收。电子顺磁共振（EPR）研究证据表明，组胺不与酶活性中心的铜相互作用。在与组胺相互作用期间，酶的抗原特性会发生变化。组胺会增加人和大鼠血清中该酶的氧化酶活性，并对肝豆状核变性患者的酶活性产生多种影响。给大鼠注射组胺后，酶活性增加，而血清中的铜浓度并未同时增加，即没有新合成铜蓝蛋白。所获得的数据表明，铜蓝蛋白可能是一种别构酶，而组胺是其正别构效应剂。
