Abstract
The plasma concentration of serum amyloid A (SAA), a plasma apolipoprotein mainly associated with high-density lipoproteins (HDL ), is increased by up to lOOO-fold as a response to certain acute phase reactions. This enormous increase can be used in the diagnosis of acute allograft rejection [l-3]. SAA, which consists of 104 amino acids, is also believed to be the precursor of the 76-amino-acid amyloid A (AA) protein found in tissue deposits of patients with secondary amyloidosis [4,5]. SAA exists in plasma in several isoforms [6-g]. Two of them, named SAA1 and SAA2 by Benditt and Eriksen [lo], represent the prominent forms. SAA, and SAA, differ in their aminoterminal arginine residue, which is missing in SAA*, giving rise to a p1 value of 0.5 lower than that of SAA,. We have developed a rapid method to isolate both SAA, and SAA, isoforms from human plasma by a combination of ultracentrifugation and fast protein liquid chromatography (FPLC ), using a Mono Q HR lO/lO preparative anionexchange column.
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