Polymorphism of tissue and serum amyloid A (AA and SAA) proteins in the mouse

J Immunol. 1978 Jul;121(1):138-40.

Abstract

Amino acid sequence studies of the amino terminal 25 residues of amyloid A (AA) protein and the serum precursor (SAA) induced with casein or LPS indicate differences in the sequence at position 6 and significant heterogeneity at several other positions in SAA. These findings suggest that SAA is a polymorphic serum protein and raise the possibility that only certain forms of SAA are processed to the tissue amyloid fibril.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Amyloid* / analysis
  • Amyloid* / metabolism
  • Amyloidosis / blood
  • Animals
  • Chromatography, Gas
  • Chromatography, Thin Layer
  • Electrophoresis, Polyacrylamide Gel
  • Liver / metabolism
  • Mice
  • Mice, Inbred Strains
  • Molecular Weight
  • Polymorphism, Genetic*
  • Protein Precursors / analysis
  • Protein Precursors / blood
  • Spleen / metabolism

Substances

  • Amino Acids
  • Amyloid
  • Protein Precursors