Abstract
When high density lipoproteins (HDL) with high contents of serum amyloid A proteins (SAA) were incubated with polymorphonuclear leucocytes (PMNL), SAA contentents in HDL protein fractions decreased markedly without significant alterations in apo A-I, A-II proteins and lipid contents. It suggests that SAA in HDL is more easily degraded than other HDL apoproteins through different metabolic pathways. Although three kinds of the isoproteins of SAA were found in the HDL from some patients in acute phases other than SAA1 and SAA2 in a previous experiment, a precursor-product relationship was not proven among these isoproteins.
