A reassessment of structure-function relationships in glucagon. Glucagon1-21 is a full agonist.
Open Access
- 1 September 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (18) , 6338-6340
- https://doi.org/10.1016/s0021-9258(19)46936-6
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Conformational transitions of glucagon in solution: The α → β transitionBiochemical and Biophysical Research Communications, 1977
- Conformation of glucagon. Predictions and consequencesBiochemistry, 1975
- Structure-function relations in glucagon. Properties of highly purified Des-his1-, monoiodo-, and [Des-Asn28,Thr29](homoserine lactone27)-glucagonBiochemistry, 1975
- A highly sensitive adenylate cyclase assayAnalytical Biochemistry, 1974
- Conformational and Biological Properties of Partial Sequences of GlucagonCanadian Journal of Physiology and Pharmacology, 1973
- The Reaction of Glucagon with Its Receptor: Evidence for Discrete Regions of Activity and Binding in the Glucagon MoleculeProceedings of the National Academy of Sciences, 1971
- Partition chromatography of glucagon and secretin on SephadexJournal of Chromatography A, 1971
- The circular dichroism of glucagon solutionsArchives of Biochemistry and Biophysics, 1969
- Isolation of an organ specific protein antigen from cell-surface membrane rat liverBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951