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• W1965645499 abstract "The hinge region of a recombinant-DNA-produced human IgG1 (Campath 1H) is specifically cleavable at a single copper-sensitive peptide bond, yielding a distinct fragment resolved by size-exclusion high-performance liquid chromatography. This novel metal ion-catalysed cleavage at slightly alkaline pH is inhibited by EDTA and its rate is reduced at slightly acidic conditions (pH 5-6) and accelerated by increasing concentrations of cupric ion and higher temperature. Complete cleavage was observed after incubation at pH 8 for 24 h with 1 mM CuCl2. Sequence analysis determined the cleavage site to be the Lys226-Thr227 bond in the hinge-region sequence DKTHT. Cleavage of other IgGs was observed to varying degrees, and specific cleavage of synthetic peptides containing this pentapeptide sequence was also observed." @default.
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• W1965645499 date "2009-01-12" @default.
• W1965645499 modified "2023-09-26" @default.
• W1965645499 title "Specific cleavage of immunoglobulin G by copper ions" @default.
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• W1965645499 doi "https://doi.org/10.1111/j.1399-3011.1996.tb01105.x" @default.
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