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Phylogenetic Analysis of Amyloid a Protein

  • Barbara Kluve-Beckerman
  • Merrill D. Benson
  • Francis E. Dwulet
  • Stephen P. DiBartola
  • M. Douglas Benson
Chapter

Abstract

Serum amyloid A (SAA) is the precursor of human reactive amyloid (AA). In addition, most forms of amyloid in other species whether spontaneous or induced by chronic inflammatory stimuli have been shown to be composed chiefly of protein AA. SAA is an apolipoprotein which has been identified in many mammalian species. To date the rat is the only mammal that has been found to lack SAA. Structural analyses have shown a strikingly high degree of sequence identity among the SAA and AA proteins of various species. All of the AA proteins examined thus far, which include those from human, monkey, mouse, mink, guinea pig, and duck, have exactly the same sequence from residue 33 through residue 45 (1). The amino and carboxyl regions of these proteins, however, are clearly more heterogeneous than their middle portions (residues 33–63).

Keywords

Amyloid Fibril Human Sequence Guanidine Hydrochloride Cyanogen Bromide Amyloid Fibril Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Barbara Kluve-Beckerman
    • 1
    • 2
  • Merrill D. Benson
    • 1
    • 2
  • Francis E. Dwulet
    • 1
    • 2
  • Stephen P. DiBartola
    • 1
    • 2
  • M. Douglas Benson
    • 1
    • 2
  1. 1.Departments of Medicine and Medical GeneticsIndiana University School of Medicine, VAMCIndianapolisUSA
  2. 2.College of Veterinary MedicineOhio State UniversityColumbusUSA

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