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- W2896471034 abstract "The luminescence characteristics of human immunoglobulins (IgGand IgM), their light and heavy chains, their Fc and (Fab)2 fragmentsand of concanavalin A were studied at room temperature and at 77K.The intrachain disulphide bonds were shown to quench the luminescenceof immunoglobulins, the effect being more pronounced at room temperature.The interchain and the intersubunit disulphide bonds affectedthe luminescence only very slightly. Algebraic addition of theluminescence properties of the fragments did not lead to recovery ofthe luminescence properties of the IgG molecules. The luminescencecharacteristics of IgG and IgM, and concanavalin A depend on the nativestructures of these proteins; it was found that the proteins tendedto acquire the intrinsic luminescence of tryptophan on denaturation.The antibodies and the concanavalin A molecule showed pH-dependentluminescence properties. [Continues.]" @default.
- W2896471034 created "2018-10-26" @default.
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- W2896471034 date "1976-01-01" @default.
- W2896471034 modified "2023-09-27" @default.
- W2896471034 title "The luminescence properties of human immunoglobulin" @default.
- W2896471034 hasPublicationYear "1976" @default.
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