The primary structure of mu-chain-disease protein BOT. Peculiar amino-acid sequence of the N-terminal 42 positions

Hoppe Seylers Z Physiol Chem. 1984 Jan;365(1):105-18. doi: 10.1515/bchm2.1984.365.1.105.

Abstract

The complete primary structure of the mu heavy-chain disease (mu-HCD) protein BOT has been determined. The monomeric HCD-mu-chain consists of 391 amino-acid residues, lacking the VH and mu CH1 domains but including the entire CH2, CH3 and CH4 domains (349 residues). The sequence of the preceding 42 N-terminal residues which we designate as the "pre-C-part" presents no homology to any known variable or constant immunoglobulin sequence, but contains an internal homology of positions 10-19 to positions 20-29. The origin of the "pre-C-part" structure and the deletion of the mu CH1 domain of protein BOT are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Chemical Phenomena
  • Chemistry
  • Chymotrypsin
  • Cyanogen Bromide
  • Heavy Chain Disease / blood*
  • Humans
  • Hydrolysis
  • Immunoglobulin Heavy Chains*
  • Immunoglobulin gamma-Chains*
  • Immunoglobulin mu-Chains
  • Peptide Fragments / analysis
  • Trypsin

Substances

  • Amino Acids
  • IGHM protein, human
  • Immunoglobulin Heavy Chains
  • Immunoglobulin gamma-Chains
  • Immunoglobulin mu-Chains
  • Peptide Fragments
  • Chymotrypsin
  • Trypsin
  • Cyanogen Bromide