Reversible conformational changes of plasmalemmal glycoproteins.

Repeated incubations of human red blood cells in low ionic isotonic sucrose result in an instantaneous agglutination. In the same medium which had caused the agglutination, erythrocytes completely disagglutinate within 60 to 90 min. Disagglutination is accompanied by the efflux of cellular ions, which causes a 500-fold increase of extracellular K+. Decomposition of agglutinates occurs at once upon addition to the medium of about 3 mM KCL. It will be inhibited for hours, if the medium is renewed twice an hour. Erythrocytes washed successively with phosphate buffered saline and isotonic sucrose are devoid of adhering blood plasma proteins. If these cells were fixed with glutaraldehyde in isotonic sucrose they had lost a) their anisotropic staining with toluidine blue, and b) most of their colloidal iron binding capacity. The staining with ruthenium red and the electrophoretic velocity of these erythrocytes apparently were identical with the controls. The findings are considered evidence of the reversible unfolding of glycocalyx glycoproteins in the low ionic medium.