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The purpose of this investigation was to examine the metabolism and inactivation of gastrin releasing peptide 10 (GRP10) by endopeptidase-24.11 prepared from the stomach wall. GRP10 was metabolized in vitro by gastric endopeptidase-24.11. The metabolites were purified by high-pressure liquid chromatography and identified as (1-8) GRP10 and (9-10) GRP10 by amino acid analysis, indicating hydrolysis of the His8-Leu9 bond. The intravenous administration of GRP10 to conscious dogs stimulated gastrin release, gastric acid secretion, pancreatic protein secretion and pancreatic bicarbonate secretion. Incubation of GRP10 with endopeptidase-24.11 significantly diminished the biological activity of the digests compared to control digests containing heat-inactivated enzyme. This effect was abolished by the enzyme inhibitor phosphoramidon. It is concluded that endopeptidase-24.11 from the stomach metabolizes and inactivates GRP10.
N W Bunnett, and
A J Turner, and
H T Debas
May 1988,
FEBS letters,
N W Bunnett, and
A J Turner, and
H T Debas
February 1985,
Biochemical Society transactions,
N W Bunnett, and
A J Turner, and
H T Debas
March 1988,
Gastroenterology,
N W Bunnett, and
A J Turner, and
H T Debas
January 1986,
Biomedica biochimica acta,
N W Bunnett, and
A J Turner, and
H T Debas
May 1993,
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N W Bunnett, and
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H T Debas
November 1992,
Regulatory peptides,
N W Bunnett, and
A J Turner, and
H T Debas
August 1996,
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N W Bunnett, and
A J Turner, and
H T Debas
August 1993,
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N W Bunnett, and
A J Turner, and
H T Debas
January 1995,
Peptides,
N W Bunnett, and
A J Turner, and
H T Debas
August 2017,
Gastroenterology research,
