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Properties of amidinated glucagons.
- Source :
-
European journal of biochemistry [Eur J Biochem] 1980 Oct; Vol. 111 (1), pp. 11-6. - Publication Year :
- 1980
-
Abstract
- Porcine glucagon has been reacted with a series of alkyl imidates. The epsilon-amino group and both the alpha and epsilon-amino groups were modified and the subsequent glucagon derivatives were purified by ion-exchange chromatography and characterized. The modified glucagons were compared with native glucagon in their ability to activate hepatic adenylate cyclase and to compete with 125I-glucagon for binding to sites specific for glucagon in hepatic plasma membranes. N epsilon-acetamidino-glucagon was as biologically potent, in both activity and binding, as native glucagon, whereas N epsilon-4-hydroxyphenylamidinoglucagon required a twofold higher concentration to obtain similar levels. These findings suggest that modification through the epsilon-amino group with alkyl imidates possessing reporter groups should result in glucagon derivatives with significant biological potency, thus providing a new approach to the study of this peptide hormone. Amidination of both epsilon and alpha-amino groups resulted in glucagon derivatives which were agonists with respect to adenylate cyclase activation and which displayed unexpected anomylous behavior on chromatography.
- Subjects :
- Adenylyl Cyclases metabolism
Amidines metabolism
Amidines pharmacology
Amino Acids analysis
Animals
Binding Sites
Binding, Competitive
Cell Membrane enzymology
Glucagon chemical synthesis
Glucagon metabolism
Glucagon pharmacology
Liver enzymology
Rats
Swine
Amidines chemical synthesis
Glucagon analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 0014-2956
- Volume :
- 111
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- European journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7439177
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1980.tb06070.x