Interaction of heavy and light chains of myeloma immunoglobulin with pooled normal chains: Quantitative analysis of association and restoration of idiotype

Ibraghimov, Alexander; Rokhlin, Oskar V.

doi:10.1016/0165-2478(85)90055-0

Cited by 2 publications

(2 citation statements)

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“…Myeloma, hybridoma and normal serum lg were obtained by precipitation of ascitic fluids and normal sera of mice and rats at 18% saturation of sodium sulfate followed by DEAE chromatography as described (1 ). Ig purity was checked by 80S-polyacrylamide gel electrophoresis (9) and isoelectric focussing (10).…”

Section: Methodsmentioning

confidence: 99%

“…Our early observation using polyclonal antibodies (Ab) was that reduction ofH-L S-S bridges of mouse myeloma lgG 1 MOPC 21 followed by separation and reassociation of H and L chains did not disturb antigenic structure ofH and L chain C domains as well as the unique quaternary V domain structure (idiotype) of the reconstituted IgG (1). Monoclonal hybridoma IgG 1 after the same treatment also retained quaternary idiotypic structure as well as specific Ab activity (2).…”

Section: Appearance Of Neoantigen In Mouse Igg1 Upon Reduction Of Intmentioning

confidence: 96%

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Appearance of Neoantigen in Mouse IgG1 Upon Reduction of Interchain Disulfide Bridges: Assessment of Local and General Conformational Rearrangements Using Monoclonal Antibody and Small-angle X-ray Scattering

Ibraghimov

Jackubov

Kayushina

et al. 1987

Journal of Biomolecular Structure and Dynamics

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Mouse hybridoma antibody E5D2 reacting with murine mono- and polyclonal IgG1 has been produced. MonAb E5D2 recognizes the antigenic determinant (epitope) buried in intact IgG1 and expressed upon mild reduction of interchain S-S bridges. Neither H nor L chains alone maintain epitope E5D2. Reassociation of gamma 1 chains (H chains of IgG1) with L chains results in complete restoration of this antigenic determinant. The data strongly suggest that epitope E5D2 depends on the quaternary structure of IgG1. The epitope is also expressed by reduced F(ab)2 fragment of IgG1 but is not connected with its antigen binding site. The likely localization of the epitope E5D2 is the interface between CH and CL domains. The second produced monAb F6C2 reacts with CH1-CL region of reduced mouse IgG2. Small-angle X-ray scattering experiments have demonstrated pronounced decrease of the radius of gyration of reduced IgG1 as compared to the intact one. This indicates general conformational changes of IgG1 molecule following mild reduction of Fab region S-S groups. Epitope E5D2 is the first quaternary antigenic subclass specific determinant described for C the region of mouse IgG. Thus, serologic expression of epitope E5D2 reveals precise conformational perturbations of small area near reduced S-S bridges while small-angle scattering demonstrates accompanying general transformation of IgG structure.

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Section: Methodsmentioning

confidence: 99%

Section: Appearance Of Neoantigen In Mouse Igg1 Upon Reduction Of Intmentioning

confidence: 96%