Isolation and incorporation into lipid vesicles of a concanavalin A receptor from human erythrocytes.

Affinity chromatography has been used to isolate a concanavalin A receptor portion of Band 3 from humen erythrocytes in the presence of the readily-dialysable detergent, dodecyltrimethylammonium bromide. Addition of phospholipids to the isolated fraction and removal of detergent by dialysis leads to formation of vesicles containing the receptor. Intramembranous particles similar in size and shape to those seen in intact erythrocytes are a characteristic of the reconstituted preparations. Vesicles containing receptor bind concanavalin A with high affinity.