Abstract
The desialylated human chorionic gonadotropin α- and β-subunits were combined with their native complementary subunits and the thyrotropic activities of the recombinants were compared to those of native and desialylated human chorionic gonadotropin using human thyroid membranes. All the combined forms interacted with the thyrotropin receptor-adenylate cyclase system, but only those with sialic acid residues present on the α-subunit were able to activate the enzyme. These data support the concept that the α-subunit contains the domain through which this hormone activates adenylate cyclase.
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