Glucagon primary sequence

Over 50% of the aspartic acid of the proteins of hepatic origin is liberated in 16 hours, but the gamma-globulins of extrahepatic origin required 36 hours to reach 50%. The extent to which this reflects certain characteristics of the primary structure is described in similar studies on insulin, ribonuclease, and glucagon (37). The cleavage of the peptide chain at the aspartic acid bonds may release other amino acids when they are between aspartic acid residues, when the aspartic acid is penultimate at either end of the chain, or if the other residues occupy positions of particularly labile sequences not known at this time. The... 

Another method of analysis which may provide useful clues to the intermolecular forces involved in the glucagon-receptor complex is a comparison of the primary structures of glucagon and a very similar peptide hormone, secretin. The sequences of the two hormones are ... 

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