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- W1991567502 abstract "Haemolytic pig IgM and pig IgM anti-Salmonella complexed with their particulate antigens showed a very large increase in complement fixing ability compared with uncomplexed pig IgM. When pig IgM was reduced with low molarities of dithiothreitol many of its inter-μ-chain disulphide bridges were cleaved but it was still held together as a 19 S molecule by non-covalent bonds. Compared to the original IgM this non-covalently bonded material had a similar ability to agglutinate erythrocytes or salmonella and these complexes had similar efficiencies of fixing complement. A significant loss of agglutinating and complement fixing ability was observed when the non-covalently bonded pentameric 19 S IgM was irreversibly dissociated into oligomers, monomers and half subunits. 7-S subunits which consisted mainly of non-covalently interacting half subunits (only μ-L disulphide bridges intact) had no or very little agglutinating ability and did not fix complement. At no stage of the reduction of pig IgM with dithiothreitol were workable amounts of completely covalently bonded 7-S subunits (all inter-chain bridges intact) released in aqueous solution. Our results indicate that reduction of 19 S IgM has little affect on biological activity providing a pentameric structure is maintained. Disruption of the pentamer either by further reduction or dissociation causes a significant loss of activity." @default.
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- W1991567502 date "1977-09-01" @default.
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- W1991567502 title "The effect of dithiothreitol on agglutination and complement Fixation by porcine 19 S IgM" @default.
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- W1991567502 doi "https://doi.org/10.1016/0005-2795(77)90149-0" @default.
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