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Matches in SemOpenAlex for { <https://semopenalex.org/work/W2005384722> ?p ?o ?g. }

• W2005384722 endingPage "274" @default.
• W2005384722 startingPage "265" @default.
• W2005384722 abstract "We have shown that human secretory component (SC) binds in vitro to different samples of human and murine dimeric immunoglobulin A (IgA). The binding ratio in the IgA/SC complex is 1:1. IgA which is stably bound to SC is separated from unreacted IgA by anion exchange chromatography. A part of IgA/SC complexes formed in vitro is unstable to this elution; the proportion varies between different samples of IgA; it increases following prolonged incubation of IgA at 37 degrees C. Incubation of IgA with glutathione/glutathione disulfide (GSH/GSSG) redox buffers increases the proportion able to form a stable complex with SC to approximately 90%. The presence of bound SC is not essential for this process but does allow it to occur at a lower GSH/GSSG concentration. The stable IgA/SC complex consists of a structure with a disulfide bond between IgA and SC apparently in equilibrium with a structure in which this bond is absent. The proportion bound covalently is similar for different samples of IgA and is insensitive to incubation with GSH/GSSG. It is significantly greater for secretory IgA (sIgA) and for IgA and SC incubated together with a starting mixture of cysteine/cystine. Monoclonal, antigen-specific IgA, all of which is optimally bound to SC in essentially the same way as in native sIgA, can be isolated in high yield. Our results support a mechanism for optimal binding of IgA to SC, that can occur both in vitro and in vivo, in which a thiol disulfide interchange occurs between a free IgA thiol and a sensitive SC disulfide following the initial non-covalent interaction." @default.
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• W2005384722 date "1998-12-01" @default.
• W2005384722 modified "2023-10-15" @default.
• W2005384722 title "Thiol–disulfide redox buffers maintain a structure of immunoglobulin A that is essential for optimal in vitro binding to secretory component" @default.
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• W2005384722 doi "https://doi.org/10.1016/s0167-4838(98)00239-8" @default.
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