Cyclic-AMP-dependent phosphorylation of glicentin

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

doi:10.1007/BF01122224

Cyclic-AMP-dependent phosphorylation of glicentin

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

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

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.

Original language	English
Pages (from-to)	489-496
Number of pages	8
Journal	Bioscience Reports
Volume	4
Issue number	6
DOIs	https://doi.org/10.1007/BF01122224
Publication status	Published (in print/issue) - Jun 1984

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title = "Cyclic-AMP-dependent phosphorylation of glicentin",

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.",

author = "Conlon, {J. M.} and L. Thim and Moody, {A. J.} and S{\"o}ling, {H. D.}",

year = "1984",

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T1 - Cyclic-AMP-dependent phosphorylation of glicentin

AU - Conlon, J. M.

AU - Thim, L.

AU - Moody, A. J.

AU - Söling, H. D.

PY - 1984/6

Y1 - 1984/6

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0021229957&partnerID=8YFLogxK

U2 - 10.1007/BF01122224

DO - 10.1007/BF01122224

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SN - 0144-8463

VL - 4

SP - 489

EP - 496

JO - Bioscience Reports

JF - Bioscience Reports

IS - 6

ER -

Cyclic-AMP-dependent phosphorylation of glicentin

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