Evidence for alpha-1-acid glycoprotein populations of different pI values after concanavalin A affinity chromatography. Study of their evolution during inflammation in man.
Isoelectric focusing in polyacrylamide gel was used to reveal the two alpha 1-acid glycoprotein populations separated by affinity chromatography on Con A-Sepharose from human purified alpha 1-acid glycoprotein, whole normal serum and sera from patients undergoing an acute inflammatory process. The concanavalin A non-reactive peak had a lower isoelectric point than did the concanavalin A reactive peak. Moreover, crossed immunoaffinity electrophoresis with free concanavalin A revealed three alpha 1-acid glycoprotein populations (concanavalin A reactive, weakly and non-reactive). A significant difference was observed between the patterns of normal and of inflammatory sera, since the concanavalin A reactive fraction was enhanced during the inflammatory process. These results suggest a variation in relative ratios of the different types of peripheral oligosaccharide branches in the alpha 1-acid glycoprotein populations.
D002846:Chromatography, Affinity; D003208:Concanavalin A; D006801:Humans; D007249:Inflammation / Q000097:blood*; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D009961:Orosomucoid / Q000302:isolation & purification*
D009961:Orosomucoid; D003208:Concanavalin A