Structural requirements for glucagon receptor binding and activation of adenylate cyclase in liver. Study of chemically modified forms of the hormone, including N alpha-trinitrophenyl glucagon, an antagonist.

摘要: Abstract The ability of several chemically modified forms glucagon to activate adenylate cyclase have been compared with their displace 125I-glucagon from specific membrane binding sites. results demonstrate that both NH2-terminal and COOH-terminal portions the peptide, as well central region molecule, are all involved in receptor subsequent activation cyclase. Receptor was very sensitive chemical modification polar residues glucagon. For example, conversion sole lysine residue homoarginine resulted over a 2-fold loss receptor-binding affinity. Loss at least great for derivatives. In case derivatives COOH terminus, correlated binding. general, however, greater than This difference greatest derivative N alpha-trinitrophenyl where about 100-fold behaved an antagonist