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[Binding of IgG and its aggregates to human platelets can be made saturable by using deoxyglucose and antimycin A]
Binding of bisdiazoniumbenzidine cross-linked (BDB) and monomeric IgG to washed human platelets at 37 degrees C was assessed. Metabolic inhibitors and prostaglandin E1 permitted study of partially reversible and saturable binding of the ligands to platelets: in presence of 0.25 microM antimycin A and 6 mM deoxyglucose, maximal binding of 3H-BDB-IgG (10 min, 37 degrees C) was 0.52 fg per platelet and of 3H-IgG (20 min, 37 degrees C) 0.13 fg per platelet. In presence of 6 mM glucose, however, the amount of IgG bound per platelet was higher and not saturable. These findings suggest that IgG is actively engulfed by the platelets.
Binding of bisdiazoniumbenzidine cross-linked (BDB) and monomeric IgG to washed human platelets at 37 degrees C was assessed. Metabolic inhibitors and prostaglandin E1 permitted study of partially reversible and saturable binding of the ligands to platelets: in presence of 0.25 microM antimycin A and 6 mM deoxyglucose, maximal binding of 3H-BDB-IgG (10 min, 37 degrees C) was 0.52 fg per platelet and of 3H-IgG (20 min, 37 degrees C) 0.13 fg per platelet. In presence of 6 mM glucose, however, the amount of IgG bound per platelet was higher and not saturable. These findings suggest that IgG is actively engulfed by the platelets.