A 25,000 molecular weight protein constituent of human amyloid fibrils related to amyloid protein AA

Jane B. Lian, Merrill Benson, Martha Skinner, Alan S. Cohen

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Amyloid fibrils from a patient with diffuse amyloid disease are dissociated in 6 m guanidine hydrochloride and fractionated by gel chromatography. Two major components are separated on Sepharose 6B. Both proteins are characterized by chromatography, immunodiffusion, discontinuous gel electrophoresis, amino acid tryptic peptide mapping and amino acid sequence analysis. The smaller of the two components is typical of the known protein AA by size (8400 daltons), amino acid composition and a 30-residue N-terminal sequence. The larger of the components (25,000 daltons) undergoes electrophoresis as a single band and appears unaffected by thiol reduction. It differs from protein AA in amino acid content and by its tryptic peptide map, although it contains an N-terminal amino acid sequence identical to protein AA when carried to 20 residues. Treatment of this larger component by mild acid hydrolysis results in the release of the 8400-dalton protein AA. Fractionation after guanidine hydrochloride treatment of this particular amyloid fibril preparation is compared to the fractionation of a typical secondary amyloid preparation that contains only protein AA as the major component. The origin and relationship of the 8,400- and 25,000-dalton protein components is discussed.

Original languageEnglish (US)
Pages (from-to)197-205
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume171
Issue number1
DOIs
StatePublished - 1975
Externally publishedYes

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Serum Amyloid A Protein
Amyloid
Molecular Weight
Molecular weight
Amino Acids
Proteins
Guanidine
Fractionation
Chromatography
Electrophoresis
Gels
Peptides
Peptide Mapping
Immunodiffusion
Protein Sequence Analysis
Sulfhydryl Compounds
Sepharose
Gel Chromatography
Amino Acid Sequence
Hydrolysis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A 25,000 molecular weight protein constituent of human amyloid fibrils related to amyloid protein AA. / Lian, Jane B.; Benson, Merrill; Skinner, Martha; Cohen, Alan S.

In: Archives of Biochemistry and Biophysics, Vol. 171, No. 1, 1975, p. 197-205.

Research output: Contribution to journalArticle

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