Mu heavy-chain disease--a defect in immunoglobulin assembly. Structural studies of the kappa chain.
Mu-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 kappa 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 mu and L chains are briefly discussed.
D000595:Amino Acid Sequence; D001536:Bence Jones Protein / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D006362:Heavy Chain Disease / Q000276:immunology*; D006801:Humans; D007143:Immunoglobulin Heavy Chains / Q000032:analysis; D007147:Immunoglobulin Light Chains / Q000032:analysis; D007145:Immunoglobulin kappa-Chains / Q000032:analysis; D007148:Immunoglobulin mu-Chains / Q000032:analysis; D008970:Molecular Weight
D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D007148:Immunoglobulin mu-Chains; D001536:Bence Jones Protein