title: [Allosteric regulation of ceruloplasmin activity].
abstract: 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.
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D002570:Ceruloplasmin / Q000276:immunology / Q000378:metabolism*; D003300:Copper / Q000097:blood; D004578:Electron Spin Resonance Spectroscopy; D006632:Histamine / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D051381:Rats
chemical_list: D003300:Copper; D006632:Histamine; D002570:Ceruloplasmin
vernacular_title: Allostericheskaia reguliatsiia aktivnosti tseruloplazmina.