Primary structure of the variable region of a human λVI light chain

Bence Jones protein SUT

B. Frangione, T. Moloshok, Alan Solomon

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

To ascertain if λVI light chains have unique structural features that account for the preferential association of these proteins with primary or multiple myeloma-related amyloidosis (amyloidosis AL) we have determined the complete amino acid sequence of the variable (V) region of the λVI Bence Jones protein SUT. This protein, obtained from a patient with amyloidosis AL, represents a complete light chain consisting of 216 residues and it has structural and serologic properties characteristic for λVI light chains. The sequence of the joining segment (J) (positions 100 to 111) of protein SUT is identical to that of the J(λI) segment of the mouse IGλ light chain gene. V region SUT is closely homologous in sequence to that of another λVI amyloid fibrillar protein, AR, differing by 21 residues. The V regions of proteins SUT and AR contain a two-residue insertion at positions 68 and 69 that has also been found in two other λVI human light chains but not in the λ-chains of other V region subgroups.

Original languageEnglish (US)
Pages (from-to)2490-2493
Number of pages4
JournalJournal of Immunology
Volume131
Issue number5
StatePublished - Dec 1 1983
Externally publishedYes

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Bence Jones Protein
Light
Amyloidosis
Proteins
Amyloidogenic Proteins
Sequence Homology
Multiple Myeloma
Amino Acid Sequence
Genes

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Primary structure of the variable region of a human λVI light chain : Bence Jones protein SUT. / Frangione, B.; Moloshok, T.; Solomon, Alan.

In: Journal of Immunology, Vol. 131, No. 5, 01.12.1983, p. 2490-2493.

Research output: Contribution to journalArticle

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AB - To ascertain if λVI light chains have unique structural features that account for the preferential association of these proteins with primary or multiple myeloma-related amyloidosis (amyloidosis AL) we have determined the complete amino acid sequence of the variable (V) region of the λVI Bence Jones protein SUT. This protein, obtained from a patient with amyloidosis AL, represents a complete light chain consisting of 216 residues and it has structural and serologic properties characteristic for λVI light chains. The sequence of the joining segment (J) (positions 100 to 111) of protein SUT is identical to that of the J(λI) segment of the mouse IGλ light chain gene. V region SUT is closely homologous in sequence to that of another λVI amyloid fibrillar protein, AR, differing by 21 residues. The V regions of proteins SUT and AR contain a two-residue insertion at positions 68 and 69 that has also been found in two other λVI human light chains but not in the λ-chains of other V region subgroups.

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