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• W2017889456 abstract "Intrigued by reports that the mitogenic effect of protein A on B lymphocytes was due to a direct interaction of cell surface immunoglobulin with protein A, the binding of 19 S, 8 S, and Fab mu fragments of 125I-labeled IgM isolated from porcine serum was investigated. Approx. 60% of purified 19 S porcine IgM interacted specifically with Protein A-Sepharose. Mild reduction and alkylation of 19 S IgM to yield monomeric IgM did not appear to alter its ability to bind to protein A. Elution of either molecular species of IgM from protein A and subsequent repassage over Protein A-Sepharose resulted in nearly quantitative rebinding of the IgM to protein A. Fab mu fragments prepared by digestion of 19 S IgM with pepsin exhibited binding characteristics similar to that observed for intact and monomeric IgM. These results suggest that: (1) there are at least two populations of porcine serum IgM, one that binds to protein A and one that does not; (2) these populations are not interconverting; (3) the ability of IgM to bind to protein A is not dependent on the 19 S pentameric structure extant in sera, but rather is an intrinsic property of some and not all four chain IgM protomers; and (4) a binding site for protein A on porcine IgM is localized in the Fab mu (including the C mu 2 domain) regions of the molecule." @default.
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• W2017889456 date "1984-11-01" @default.
• W2017889456 modified "2023-09-27" @default.
• W2017889456 title "Interaction of porcine immunoglobulin M with protein A of Staphylococcus aureus" @default.
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• W2017889456 doi "https://doi.org/10.1016/0167-4838(84)90287-5" @default.
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