Amino acid sequence of a kappa I primary (AL) amyloid protein (AND)

Juris J. Liepnieks, Francis E. Dwulet, Merrill Benson

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The complete amino acid sequence of amyloid protein AND is presented. Amyloid fibrils were isolated from the spleen of patient AND, and the subunit protein was isolated from the fibrils after reduction and carboxymethylation. Sequence analysis of intact protein AND identified it as a kappa I immunoglobulin light chain. The complete sequence was determined from its tryptic peptides. The protein contained the entire variable region and the constant region to position 145 of the light chain. Several unique amino acid substitutions were found in protein AND compared to other kappa I proteins. The glycine, serine, arginine, threonine, alanine and arginine at positions 31, 45, 55, 76, 85 and 107, respectively, are reported for the first time in a kappa I protein. A number of uncommon amino acid substitutions were found in the framework regions in protein AND around the contact region of the dimer which may result in the molecule becoming more susceptible to fibril formation.

Original languageEnglish
Pages (from-to)481-485
Number of pages5
JournalMolecular Immunology
Volume27
Issue number6
DOIs
StatePublished - 1990

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Amino Acid Sequence
Amino Acid Substitution
Proteins
Arginine
Immunoglobulin kappa-Chains
Amyloidogenic Proteins
Protein Sequence Analysis
Protein Subunits
Threonine
Amyloid
Alanine
Glycine
Serine
Spleen
amyloid protein AL
Light
Peptides

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Amino acid sequence of a kappa I primary (AL) amyloid protein (AND). / Liepnieks, Juris J.; Dwulet, Francis E.; Benson, Merrill.

In: Molecular Immunology, Vol. 27, No. 6, 1990, p. 481-485.

Research output: Contribution to journalArticle

Liepnieks, Juris J. ; Dwulet, Francis E. ; Benson, Merrill. / Amino acid sequence of a kappa I primary (AL) amyloid protein (AND). In: Molecular Immunology. 1990 ; Vol. 27, No. 6. pp. 481-485.
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