Abstract
Senescent human erythrocytes (RBC) are able to adhere to and be phagocytized by autologous monocytes in vitro to a greater extent than are young RBC. This adhesion and erythrophagocytosis of senescent RBC is inhibited by D-galactose, N-acetyl-D-galactosamine, their corresponding derivatives of bovine serum albumin, and lactose. On the other hand, D-glucose, D-mannose, L-fucose, N-acetyl-D-glucosamine, and their corresponding derivatives of bovine serum albumin are noninhibiting. The glycopeptides released by tryptic digestion of senescent RBC and purified on immobilized peanut agglutinin are the most effective inhibitors of both RBC adhesion and phagocytosis by autologous monocytes obtained from peripheral blood.
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