Cyclic-AMP-dependent phosphorylation of glicentin
- 1 June 1984
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 4 (6) , 489-496
- https://doi.org/10.1007/bf01122224
Abstract
Highly purified glicentin, a 69-amino-acid-residue peptide isolated from porcine intestine that contains the full sequence of glucagon and is probably biosynthetically related to glucagon, is a substrate for cyclic-AMP-dependent protein kinase in a cell-free system, Glicentin-related pancreatic peptide (residues 1–30 of glicentin) and glucagon were not phosphorylated under the same reaction conditions. It is postulated that the serine residue at position 34 of glicentin (position 2 of glucagon), that is part of the sequence Lys.Arg. His.Ser., is the probable site of phosphorylation.This publication has 19 references indexed in Scilit:
- Mammalian pancreatic preproglucagon contains three glucagon-related peptides.Proceedings of the National Academy of Sciences, 1983
- Exon duplication and divergence in the human preproglucagon geneNature, 1983
- Hamster preproglucagon contains the sequence of glucagon and two related peptidesNature, 1983
- Purification and chemical characterization of a glicentin-related pancreatic peptide (proglucagon fragment) from porcine pancreasBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem.Proceedings of the National Academy of Sciences, 1982
- Biosynthesis of phosphorylated forms of corticotropin-related peptides.Proceedings of the National Academy of Sciences, 1981
- The primary structure of porcine glicentin (proglucagon)Regulatory Peptides, 1981
- Relationship of glicentin to proglucagon and glucagon in the porcine pancreasNature, 1981
- Glicentin: A precursor of glucagon?Life Sciences, 1979
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979