Cyclic-AMP-dependent phosphorylation of glicentin

J. M. Conlon, L. Thim, A. J. Moody, H. D. Söling

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


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), t h a t is part of the sequence Lys.Arg. His.Ser., is the probable site of phosphorylation.

Original languageEnglish
Pages (from-to)489-496
Number of pages8
JournalBioscience Reports
Issue number6
Publication statusPublished (in print/issue) - Jun 1984


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