The primary structure of serum amyloid A protein in the rabbit: Comparison with serum amyloid A proteins in other species

Juris J. Liepnieks, Francis E. Dwulet, Merrill D. Benson, Barbara Kluve-Beckerman, Irving Kushner

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Rabbit serum amyloid A (SAA) protein was isolated from acute-phase serum by ultra-centrifugation, molecular seive chromatography, and ion-exchange chromatography. The complete amino acid sequence of the protein was established by sequence analysis of peptides derived from trypsin and Staphylococcus proteinase digestion of the protein. The molecule consisted of 104 amino acids and had an amino terminus that was blocked by pyrrolidonecarboxylic acid. Heterogeneity was not observed at any residue, which suggests that the material sequenced consisted of a single serum amyloid A species. The protein is highly homologous to serum amyloid A from humans and other animals, particularly in the middle portion of the molecule (positions 33 to 63), which suggests that this region may be important in its function. This highly conserved region may also contain the determinants for amyloid formation.

Original languageEnglish (US)
Pages (from-to)570-575
Number of pages6
JournalThe Journal of Laboratory and Clinical Medicine
Volume118
Issue number6
StatePublished - Dec 1991

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

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