
Pre-B lymphocytes, and hybridomas derived from them, synthesize immunoglobulin heavy (IgH) chain in the absence of light (L) chain. In the Abelson virus transformed line 18-81, which is representative of the pre-B cell stage, we observed that at least some of the H-chains are bound to a protein other than L-chain. Here we show that the protein (which we term immunoglobulin heavy-chain binding protein, BiP) binds non-covalently to free IgH, but not to IgH associated with IgL.
B-Lymphocytes, Peptide Fragments, Molecular Weight, Mice, Myeloma Proteins, Animals, Immunoglobulin Light Chains, Carrier Proteins, Immunoglobulin Heavy Chains, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Molecular Chaperones
B-Lymphocytes, Peptide Fragments, Molecular Weight, Mice, Myeloma Proteins, Animals, Immunoglobulin Light Chains, Carrier Proteins, Immunoglobulin Heavy Chains, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Molecular Chaperones
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