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μ Heavy‐Chain Disease—A Defect in Immunoglobulin Assembly Structural Studies of the χ Chain
Author(s) -
FRANGIONE B.,
FRANKLIN E. C.,
PRELLI F.
Publication year - 1976
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.1365-3083.1976.tb03011.x
Subject(s) - cysteine , monomer , bence jones protein , disulfide bond , residue (chemistry) , chemistry , immunoglobulin light chain , chain (unit) , heavy chain , stereochemistry , antibody , biochemistry , biology , enzyme , genetics , organic chemistry , gene , physics , astronomy , polymer
μ‐chain protein GLI is a pentameric molecule with an amino‐terminal deletion comprising 130 residues. The half‐cysteine residue (position 140) which forms the H‐L disulfide bridge in normal IgM is present. Instead of being joined to the L chain, it presumably exists as an additional inter‐H‐H disulfide bridge. The χ Bence Jones protein is of normal size and present in two forms: as monomers and dimers. The carboxy‐terminal half‐cysteine of the monomer is bound to cysteine. Possible reasons for failure of assembly between μ and L chains are briefly discussed.