title: Heterogeneity of human amyloid protein AA and its related serum protein, SAA.
abstract: The heterogeneity of the human amyloid proteins SAA and AA was studied. Both proteins could be separated into several fractions by ion-exchange chromatography. Amino acid analysis of the ion-exchange-chromatographed fractions of protein AA showed that the main difference was in the length of the polypeptide. Thus, it seems that the original AA preparation consists of a mixture of AA proteins with length ranging from 66 to 78 amino acid residues. By enzymatic degradation of three different forms of SAA with kallikrein, fragments were formed with a molecular weight very similar to that of protein AA.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000032:analysis*; D000686:Amyloidosis / Q000378:metabolism; D001172:Arthritis, Rheumatoid / Q000097:blood; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007610:Kallikreins; D008099:Liver / Q000032:analysis; D008970:Molecular Weight; D000685:Serum Amyloid A Protein / Q000032:analysis*
chemical_list: D000596:Amino Acids; D000682:Amyloid; D000685:Serum Amyloid A Protein; D007610:Kallikreins