Polymorphism in a kappa I primary (AL) amyloid protein (BAN)

Francis E. Dwulet, Timothy P. O'connor, Merrill D. Benson

Research output: Contribution to journalArticle

34 Scopus citations


In an attempt to understand the relationship of amino acid sequence to the formation of primary or multiple myeloma-related amyloid (AL amyloid), we have determined the complete amino acid sequence of amyloid protein BAN. This protein belongs to the kappa I immunoglobulin light chain subgroup and has a polypeptide chain length of 126 amino acids. It encompasses the entire variable region, the joining segment and the first tryptic peptide of the constant region. This protein has two unique features. First, the molecule is glycosylated. At position 61 the usual arginine residue has been replaced by an asparagine with the generation of the signal sequence Asn-Phe-Thr, to which a glucosaminecontaining carbohydrate unit is attached. Secondly, the protein is not monoclonal but consists of two chains which have the same variable region but different J-segments. Comparison of the BAN sequence with other amyloid and nonamyloid kappa I proteins reveals a systematic difference between the two groups. In the amyloid proteins, several hydrophilic framework residues have been replaced by hydrophobic residues. These substitutions may provide the nucleation sites for self-aggregation and fibril formation.

Original languageEnglish (US)
Pages (from-to)73-78
Number of pages6
JournalMolecular Immunology
Issue number1
StatePublished - Jan 1986

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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