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The amino acid sequence of protein AA from a burro (Equus asinus).

Abstract: The primary structure of amyloid fibril protein AA of a burro has been determined by Edman degradation. The 80 amino acid residue long protein shows strong resemblance to that of other mammalian AA-proteins and differs from equine protein AA at 5 positions: Burro/horse positions 20 (Q/N), 44 (R,Q, K/K,Q), 59 (G,L/G,A), 61 (Q/E) and 65 (N/R).
Publication Date: 2003-12-03 PubMed ID: 14640027DOI: 10.3109/13506120308998995Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article outlines the successful determination of the primary structure of amyloid fibril protein AA of a burro (Equus asinus) using the Edman degradation process. It also highlights similarities and differences between this protein and that of other mammals, with specifics on the dissimilarities between burro and horse proteins.

Amyloid Fibril Protein AA Structure Determination

  • The research focuses on determining the structure of amyloid fibril protein AA, a significant protein notably found in burros (Equus asinus).
  • The researchers used the Edman degradation method to breakdown the protein and determine its structure. Edman degradation is a chemical process used to sequence the amino acids in a peptide. In this process, one amino acid at a time is cleaved from the amino terminus (start) of the protein and identified.

Comparative Analysis of Protein Structures

  • Following the determination of the protein structure, the researchers compared it with the AA proteins of other mammals. The core objective was to decode how much the burro’s protein resembles other mammalian AA proteins.
  • The results indicated a strong resemblance between the burro’s AA protein and other mammalian AA proteins, implying similarities in their biochemical and physiological functions.

Comparison between Burro and Horse Proteins

  • The study also highlighted the differences between the AA proteins of burros and horses. Specifically, the variations were noted at five positions: 20 (Q/N), 44 (R,Q, K/K,Q), 59 (G,L/G,A), 61 (Q/E) and 65 (N/R).
  • This implies that while the proteins share a significant degree of similarity, certain structural and functional differences may exist between species, possibly affecting their physiological roles.

Cite This Article

APA
Sletten K, Johnson KH, Westermark P. (2003). The amino acid sequence of protein AA from a burro (Equus asinus). Amyloid, 10(3), 144-146. https://doi.org/10.3109/13506120308998995

Publication

ISSN: 1350-6129
NlmUniqueID: 9433802
Country: England
Language: English
Volume: 10
Issue: 3
Pages: 144-146

Researcher Affiliations

Sletten, Knut
  • Department of Biochemistry/Biotechnology Centre of Oslo, University of Oslo, Norway.
Johnson, Kenneth H
    Westermark, Per

      MeSH Terms

      • Amino Acid Sequence
      • Animals
      • Equidae / genetics
      • Female
      • Liver / chemistry
      • Molecular Sequence Data
      • Protein Structure, Tertiary
      • Sequence Analysis
      • Serum Amyloid A Protein / chemistry
      • Serum Amyloid A Protein / genetics

      Citations

      This article has been cited 1 times.
      1. Jansson DS, Bröjer C, Neimanis A, Mörner T, Murphy CL, Otman F, Westermark P. Post mortem findings and their relation to AA amyloidosis in free-ranging Herring gulls (Larus argentatus). PLoS One 2018;13(3):e0193265.
        doi: 10.1371/journal.pone.0193265pubmed: 29494674google scholar: lookup