Identification and characterization of amyloid protein AA in spontaneous canine amyloidosis

Merrill Benson, F. E. Dwulet, S. P. DiBartola

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Amyloid fibrils were isolated from kidney tissue of a dog that presented with renal failure due to spontaneous amyloidosis. This fibril material was reduced, alkylated and chromatographed on a column of Sepharose CL6B. A major retarded fraction, when subjected to amino acid sequencing, demonstrated a blocked amino terminus. The isolated protein was then degraded with cyanogen bromide, and the resultant three peptides were isolated by high-pressure liquid chromatography. The amino acid sequence of one peptide corresponded to the sequence of human amyloid protein AA from position 17 to 23. A second peptide gave an animo acid sequence homologous to the published human protein AA sequence starting with position 24. Although a high degree of homology between canine and human AA is seen, the blocked amino terminus is similar to the AA protein of mink. These data show that spontaneous canine amyloid is analogous to human reactive (secondary) amyloid and, therefore, may aid in defining mechanisms of human amyloid pathogenesis.

Original languageEnglish
Pages (from-to)448-452
Number of pages5
JournalLaboratory Investigation
Volume52
Issue number4
StatePublished - 1985

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Serum Amyloid A Protein
Amyloidosis
Canidae
Amyloid
Peptides
Mink
Cyanogen Bromide
Proteins
Protein Sequence Analysis
Sequence Homology
Sepharose
Renal Insufficiency
Amino Acid Sequence
High Pressure Liquid Chromatography
Dogs
Kidney
Acids

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

Identification and characterization of amyloid protein AA in spontaneous canine amyloidosis. / Benson, Merrill; Dwulet, F. E.; DiBartola, S. P.

In: Laboratory Investigation, Vol. 52, No. 4, 1985, p. 448-452.

Research output: Contribution to journalArticle

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