HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wright, D. E. Articles by Rodbell, M. Search for Related Content PubMed PubMed Citation Articles by Wright, D. E. Articles by Rodbell, M. Social Bookmarking                      What's this?

JBC, Vol. 254, Issue 2, 268-269, Jan, 1979

Glucagon1-6 binds to the glucagon receptor and activates hepatic adenylate cyclase

D. E. Wright and M. Rodbell

A fragment of glucagon encompassing its first six NH2-terminal residues (His-Ser-Gln-Gly-Thr-Phe) binds to the glucagon receptor and stimulates adenylate cyclase activity in rat liver plasma membranes. Glucagon1-6 is a partial agonist since it stimulates, at saturating concentrations, to the extent of 75% of the maximal activity given by the native hormone. The binding affinity and potency of glucagon1-6 are 0.001% the native hormone. Discussed are the implications of these findings on the structure-function relationships required for the action of glucagon and for preparing clinically useful analogs of the hormone.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. G. Unson, C.-R. Wu, C. P. Cheung, and R. B. Merrifield Positively Charged Residues at Positions 12, 17, and 18 of Glucagon Ensure Maximum Biological Potency J. Biol. Chem., April 24, 1998; 273(17): 10308 - 10312. [Abstract] [Full Text] [PDF]