Glucagon structure-function relationships using isolated rat hepatocytes

Victor J. Hruby, Nirankar S. Agarwal, Ann Griffen, Marvin D. Bregman, Charles A. Nugent, Klaus Brendel

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The ability of glucagon and several of its semi-synthetic analogues to stimulate glucose production in isolated rat hepatocytes was measured and compared for relative potencies. The order of decreasing biological activities of glucagon in this assay was as follows: glucagon > [HArg12]-glucagon > [des-Asn28, Thr29][homoserinehydrazide27]-glucagon approx. equal to [des-His1]-glucagon > [des-Asn28, Thr29] [homoserinelactone27]-glucagon > [des-Asn28, Thr29]-[n-butylhomoserineamide27]-glucagon > glucagon1-21. Qualititatively, these results are similar to those obtained previously in the hepatic plasma membrane adenylate cylase assay. Minor exceptions were noted for the hydrazide derivative nd the partial agonist [des-His1]-glucagon, both of which were slightl y more potent relative to glucagon in the glycogenolytic assay than in the adenylate cyclase assay. The assay provides important insight into glucagon structure-function relationships.

Original languageEnglish (US)
Pages (from-to)383-390
Number of pages8
JournalBBA - General Subjects
Issue number3
StatePublished - May 18 1981
Externally publishedYes


  • (Rat hepatocyte)
  • Adenylate cyclase
  • Glucagon analog
  • Glycogenolysis
  • Structure-function

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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