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The primary structure of human urogastrone
International Journal of Peptide and Protein Research
|January 1, 1977
Summary
Human urogastrone, a potent gastric acid inhibitor found in urine, has been structurally characterized. It is identical to human epidermal growth factor, sharing significant sequence homology and biological activity.
Area of Science:
- Biochemistry
- Molecular Biology
- Gastroenterology
Background:
- Urogastrone, a known inhibitor of gastric acid secretion, has been isolated from human urine.
- Recent advancements allowed for its purification and detailed structural analysis.
Purpose of the Study:
- To determine the complete amino acid sequence and disulfide bond arrangement of beta- and gamma-urogastrone.
- To investigate the structural relationship between urogastrone and epidermal growth factor (EGF).
Main Methods:
- Enzymatic degradation (trypsin, chymotrypsin, thermolysin, Armillaria mellea protease) of S-carboxymethyl derivatives.
- Peptide sequencing using the dansyl Edman method.
- Partial acid hydrolysis and oxidation to identify disulfide bonds.
Main Results:
- Beta-urogastrone is a 53-amino acid polypeptide with three disulfide bonds.
- Gamma-urogastrone shares the same sequence but lacks the C-terminal arginine.
- Urogastrone is structurally homologous to mouse epidermal growth factor (EGF), with 37 common residues.
- Both peptides exhibit similar effects on gastric acid secretion and epidermal growth.
Conclusions:
- Urogastrone is identified as human epidermal growth factor (hEGF).
- Structural variations contribute to urogastrone's increased acidity compared to EGF.
- Biological activity is retained even after removal of up to six C-terminal residues.