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Cyclic-AMP-dependent phosphorylation of glicentin

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Bioscience Reports

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

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Authors and Affiliations

  1. Klinische Arbeitsgruppe für Gastrointestinale Endokrinologie der MPG, D-3400, Göttingen, FRG

    J. M. Conlon

  2. Novo Research Institute, Copenhagen, Denmark

    L. Thim & A. J. Moody

  3. Abteilung für Klinische Biochemie, Zentrum Innere Medizin, Universität Göttingen, FRG

    H. D. Söling

Authors
  1. J. M. Conlon
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  2. L. Thim
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  3. A. J. Moody
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  4. H. D. Söling
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Conlon, J.M., Thim, L., Moody, A.J. et al. Cyclic-AMP-dependent phosphorylation of glicentin. Biosci Rep 4, 489–496 (1984). https://doi.org/10.1007/BF01122224

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  • DOI: https://doi.org/10.1007/BF01122224

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