Characterization of human amyloid-related protein SAA as a polymorphic protein: association with albumin and prealbumin in serum.
Human amyloid-related protein SAA has been prepared and purified by gel filtration, ion-exchange and affinity chromatography techniques. It was shown that SAA, even after extensive purification, is an electrophoretically heterogeneous protein. In addition, prealbumin and fragments of albumin were detected in the SAA preparation. Most of the SAA molecules and the fragments of albumin were present in a free form, but some SAA was also found to be complexed with albumin fragments.
D000368:Aged; D000682:Amyloid / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004340:Drug Contamination; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008297:Male; D011228:Prealbumin / Q000032:analysis*; D012709:Serum Albumin / Q000032:analysis*; D000685:Serum Amyloid A Protein / Q000276:immunology / Q000302:isolation & purification*; D012995:Solubility
D000682:Amyloid; D011228:Prealbumin; D012709:Serum Albumin; D000685:Serum Amyloid A Protein