Disulfide bonds of human IgM: differential sensitivity to reductive cleavage

E Kownatzki - Scandinavian Journal of Immunology, 1973 - Wiley Online Library
E Kownatzki
Scandinavian Journal of Immunology, 1973Wiley Online Library
Two Waldenström Microglobulins were reduced with increasing amounts of dithiothreitol
ranging from 0.25 to 2.0 mM. Disruption of intersubunit, interchain and μ‐J chain disulfide
bonds was measured by determining the amount of IgMs, μ chains and J chains released at
a given DTT concentration. Intersubunit bonds were most labile, while S‐S bonds linking μ
and J chains were most resistant to reductive cleavage.
Two Waldenström Microglobulins were reduced with increasing amounts of dithiothreitol ranging from 0.25 to 2.0 mM. Disruption of intersubunit, interchain and μ‐J chain disulfide bonds was measured by determining the amount of IgMs, μ chains and J chains released at a given DTT concentration. Intersubunit bonds were most labile, while S‐S bonds linking μ and J chains were most resistant to reductive cleavage.
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