Chemical characterization of a lambda I amyloid protein isolated from formalin-fixed and paraffin-embedded tissue sections

Masahide Yazaki, Juris J. Liepnieks, John Callaghan, Charles E. Connolly, Merrill D. Benson

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Amyloid protein was isolated from formalin-fixed paraffin-embedded heart tissue sections from a patient with primary (AL) amyloidosis by extraction with 6 M guanidine HCl. SDS-PAGE analysis of extracted material showed a major band at 16 kDa and a minor band at 18 kDa. Edman degradation analysis before and after pyroglutamate aminopeptidase treatment showed that the amyloid protein contained N-terminal pyroglutamic acid and was derived from an immunoglobulin λ light chain. Analysis of tryptic peptides from the extract identified the amyloid protein as a λI. Of particular interest is that almost the entire amyloid protein amino acid sequence could be obtained from the cardiac sections. These results demonstrate that formalin-fixed paraffin-embedded tissue sections can be used for extensive biochemical characterization of amyloid proteins and will become a valuable source for isolation and extensive biochemical characterization of amyloid proteins as they are now a valuable source for isolation of DNA for genetic analysis.

Original languageEnglish (US)
Pages (from-to)50-55
Number of pages6
JournalAmyloid
Volume11
Issue number1
DOIs
StatePublished - Mar 1 2004

Keywords

  • λ light chain
  • Amyloid protein
  • Formalin fixed
  • Paraffin-embedded tissue section

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Medicine(all)

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