Re-evaluation of glucagon1-6: The N-terminal hexapeptide of glucagon is not biologically active in the hepatic adenylate cyclase system

John T. Pelton; Dev Trivedi; Victor J. Hruby

doi:10.1016/0024-3205(83)90012-7

Re-evaluation of glucagon_1-6: The N-terminal hexapeptide of glucagon is not biologically active in the hepatic adenylate cyclase system

John T. Pelton, Dev Trivedi, Victor J. Hruby

Chemistry and Biochemistry

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

1 Scopus citations

Abstract

The N-terminal hexapeptide of glucagon and the corresponding carboxamide analog, were prepared by solid-phase synthesis and tested for biological activity in the hepatic adenylate cyclase system. Both peptides were found to be inactive, even at concentrations of 10 mM. The differences observed in the activity of our compounds compared to previous reports, is ascribed to the presence of a contaminant found in earlier preparations which activates adenylate cyclase.

Original language	English (US)
Pages (from-to)	1307-1314
Number of pages	8
Journal	Life Sciences
Volume	33
Issue number	13
DOIs	https://doi.org/10.1016/0024-3205(83)90012-7
State	Published - Sep 26 1983

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
Pharmacology, Toxicology and Pharmaceutics(all)

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10.1016/0024-3205(83)90012-7

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title = "Re-evaluation of glucagon1-6: The N-terminal hexapeptide of glucagon is not biologically active in the hepatic adenylate cyclase system",

abstract = "The N-terminal hexapeptide of glucagon and the corresponding carboxamide analog, were prepared by solid-phase synthesis and tested for biological activity in the hepatic adenylate cyclase system. Both peptides were found to be inactive, even at concentrations of 10 mM. The differences observed in the activity of our compounds compared to previous reports, is ascribed to the presence of a contaminant found in earlier preparations which activates adenylate cyclase.",

author = "Pelton, {John T.} and Dev Trivedi and Hruby, {Victor J.}",

note = "Funding Information: ?hls work was supported, in part, by a grant from the U.S. Public Health Service (AM 21085). John T. Pelton is the recipient of the NIH Postdoctoral",

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AU - Pelton, John T.

AU - Trivedi, Dev

AU - Hruby, Victor J.

N1 - Funding Information: ?hls work was supported, in part, by a grant from the U.S. Public Health Service (AM 21085). John T. Pelton is the recipient of the NIH Postdoctoral

PY - 1983/9/26

Y1 - 1983/9/26

N2 - The N-terminal hexapeptide of glucagon and the corresponding carboxamide analog, were prepared by solid-phase synthesis and tested for biological activity in the hepatic adenylate cyclase system. Both peptides were found to be inactive, even at concentrations of 10 mM. The differences observed in the activity of our compounds compared to previous reports, is ascribed to the presence of a contaminant found in earlier preparations which activates adenylate cyclase.

AB - The N-terminal hexapeptide of glucagon and the corresponding carboxamide analog, were prepared by solid-phase synthesis and tested for biological activity in the hepatic adenylate cyclase system. Both peptides were found to be inactive, even at concentrations of 10 mM. The differences observed in the activity of our compounds compared to previous reports, is ascribed to the presence of a contaminant found in earlier preparations which activates adenylate cyclase.

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JF - Life Sciences

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ER -

Re-evaluation of glucagon_1-6: The N-terminal hexapeptide of glucagon is not biologically active in the hepatic adenylate cyclase system

Abstract

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