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Amyloid
The Journal of Protein Folding Disorders
Volume 10, 2003 - Issue 3
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Original Article

Sequence Communication: The amino acid sequence of protein AA from a burro (Equus asinus)

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Pages 144-146 | Accepted 29 May 2003, Published online: 06 Jul 2009

References

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  • Skinner M, Shirahama T, Cohen A S, Deal C L. The association of amyloid P-component (AP) with the amyloid fibril: an updated method for amyloid fibril protein isolation. Prep Biochem 1983; 12: 461–476
  • Westermark G T, Sletten K, Grubb A, Westermark P. AA-amyloidosis. Tissue component-specific association of various protein AA subspecies and evidence of a fourth SAA gene product. Am J Path 1990; 137: 377–383
  • Schagger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987; 166: 368–379
  • Samdal I A, Sletten K, Olsen K E, Westermark P. AL 366 – a glycosylated protein of kappa 1b origin in a patient with systemic amyloidosis of predominantly non-parenchymatous distribution. Amyloid: J. Protein Folding Disord. 2001; 8: 111–114
  • Gustavsson Å, Jahr H, Tobiassen R, Jacobson D R, Sletten K, Westermark P. Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis. Lab Invest 1995; 73: 703–708
  • Sletten K, Husebekk A, Husby G. The amino acid sequence of an amyloid fibril protein AA isolated from the horse. Scand J Immunol 1987; 26: 79–84

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