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Specific cleavage of immunoglobulin G by copper ions


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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 (pH5-6) 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 CuC12. 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. © Munksgaard 1996.

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