title: Long-term metastable conformation of human Fcgamma subunit.
abstract: It was found that the human (hu) myeloma IgG1 Ser, its Fcgamma fragment and the chimeric mouse-human monoclonal antibody (chim-mAb), containing the constant part of hu-gamma1-chain, can exist in a long-term metastable conformational state. This state arises as a result of short incubation of IgG molecules and their Fcgamma fragments at pH<2.8 and the consequent rapid neutralisation to pH 7.0-8.0. At pH<2.8 the three-dimensional structure of C(gamma)2 domains is unfolded, but rapidly refolds after neutralisation. At the same time, non-covalent interactions between C(gamma)2 and C(gamma)3 domains are restored very slowly. A metastable state of IgG keeps 70% of complement-binding ability in comparison with the native state.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142292, Russia. tischen@vega.protres.ru
authors.forename: Vladimir M
authors.initials: VM
authors.lastname: Tischenko
authors.forename: Vladimir P
authors.initials: VP
authors.lastname: Zav'yalov
mesh_terms: D000818:Animals; D006801:Humans; D051379:Mice; D009101:Multiple Myeloma / Q000276:immunology; D011487:Protein Conformation; D017452:Receptors, IgG / Q000737:chemistry*
chemical_list: D017452:Receptors, IgG