Adsorbed proteins mask negatively charged sites of the erythrocyte glycocalyx.

Protein masking of charged sites of the erythrocyte glycocalyx was studied by means of the colloidal iron affinity. Washed red cells were fixed with glutaraldehyde such as to stabilize their glycocalyx and to inhibit conformational changes during posttreatment. Following the incubation in an ionic protein solution, proteins adsorbed to the cell surface were insolubilized by repeated treatment with low ionic isotonic surcose. Erythrocytes coated with precipitated proteins exhibited a rough surface. Their iron binding capacity was reduced considerably. In comparison with serum albumin, masking by gamma globulin was more efficient, apparently, because of its insolubility in low ionic media. High ionic incubation of coated erythrocytes resolubilized adsorbed proteins and unmasked negatively charged groups of the glycocalyx.