Degradation of amyloid-related serum protein SAA by a component present in rabbit and human serum.
After incubation of protein SAA-containing rabbit serum at 37 degrees C overnight, the strength of the precipitation reaction against antiserum to SAA was decreased. This was at east partly due to enzymatic degradation of protein SAA. The enzymatic activity was not strongly associated with the SAA-high-density lipoprotein (HDL) complex, since it sedimented in the preparative ultracentrifuge at a density at which the SAA-HDL complex floats. The degrading component was obtained in concentrated form from rabbit and human sera by adsorption to Sepharose 4B. Degradation of human SAA by the human serum component was inhibited with disopropyl fluorophosphate, an inhibitor of serine proteases.
D000682:Amyloid / Q000276:immunology*; D000818:Animals; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D006801:Humans; D007106:Immune Sera / Q000276:immunology; D005779:Immunodiffusion; D008075:Lipoproteins, HDL / Q000097:blood / Q000276:immunology*; D011817:Rabbits; D000685:Serum Amyloid A Protein / Q000276:immunology* / Q000378:metabolism
D000682:Amyloid; D007106:Immune Sera; D008075:Lipoproteins, HDL; D000685:Serum Amyloid A Protein