Immunoglobulin heavy chain binding protein

Nature. 1983 Nov;306(5941):387-9. doi: 10.1038/306387a0.

Abstract

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.

MeSH terms

  • Animals
  • B-Lymphocytes / metabolism
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Endoplasmic Reticulum Chaperone BiP
  • Heat-Shock Proteins*
  • Immunoglobulin Heavy Chains / metabolism*
  • Immunoglobulin Light Chains / metabolism
  • Mice
  • Molecular Chaperones*
  • Molecular Weight
  • Myeloma Proteins / analysis
  • Peptide Fragments / analysis

Substances

  • Carrier Proteins
  • Endoplasmic Reticulum Chaperone BiP
  • Heat-Shock Proteins
  • Immunoglobulin Heavy Chains
  • Immunoglobulin Light Chains
  • Molecular Chaperones
  • Myeloma Proteins
  • Peptide Fragments