Premium
Disulfide Bonds of Human IgM: Differential Sensitivity to Reductive Cleavage
Author(s) -
KOWNATZKI E.
Publication year - 1973
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1973.tb02052.x
Subject(s) - dithiothreitol , cleavage (geology) , disulfide bond , chemistry , stereochemistry , biochemistry , enzyme , biology , paleontology , fracture (geology)
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.