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Title: Receptor binding and cell-mediated metabolism of (/sup 125/I)monoiodoglucagon by isolated canine hepatocytes

Abstract

A reverse-phase HPLC method has been developed to purify /sup 125/I-labeled products resulting from the chloramine-T-based iodination of glucagon. In addition the products ((/sup 125/I)iodoTyr/sup 10/ /sup 13/)glucagon, ((/sup 125/I)iodoTyr/sup 13/)glucagon, and ((/sup 125/I)iodoTyr/sup 10/)glucagon) have been used to study the receptor binding of glucagon and the cell-mediated metabolism of the hormone by isolated canine hepatocytes. It was concluded that (a) not withstanding apparent differences in affinities exhibited by the three peptides, the interactions with the glucagon receptor are functionally equivalent, and (b) the cell-mediated metabolism of receptor-bound glucagon involves the formation of hormone-derived peptides in which the biologically important NH/sub 2/-terminal region of the hormone has been modified by limited proteolytic cleavage.

Authors:
;
Publication Date:
Research Org.:
Univ. of Chicago, IL
OSTI Identifier:
5906365
Resource Type:
Journal Article
Journal Name:
J. Biol. Chem.; (United States)
Additional Journal Information:
Journal Volume: 259:14
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GLUCAGON; METABOLISM; LIVER CELLS; BIOCHEMISTRY; CHEMICAL BONDS; DOGS; IODINE 125; LABELLED COMPOUNDS; PROTEOLYSIS; RECEPTORS; TRACER TECHNIQUES; ANIMAL CELLS; ANIMALS; BETA DECAY RADIOISOTOPES; CHEMICAL REACTIONS; CHEMISTRY; DAYS LIVING RADIOISOTOPES; DECOMPOSITION; ELECTRON CAPTURE RADIOISOTOPES; HORMONES; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; MAMMALS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PEPTIDE HORMONES; PEPTIDES; POLYPEPTIDES; PROTEINS; RADIOISOTOPES; SOMATIC CELLS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Hagopian, W A, and Tager, H S. Receptor binding and cell-mediated metabolism of (/sup 125/I)monoiodoglucagon by isolated canine hepatocytes. United States: N. p., 1984. Web.
Hagopian, W A, & Tager, H S. Receptor binding and cell-mediated metabolism of (/sup 125/I)monoiodoglucagon by isolated canine hepatocytes. United States.
Hagopian, W A, and Tager, H S. 1984. "Receptor binding and cell-mediated metabolism of (/sup 125/I)monoiodoglucagon by isolated canine hepatocytes". United States.
@article{osti_5906365,
title = {Receptor binding and cell-mediated metabolism of (/sup 125/I)monoiodoglucagon by isolated canine hepatocytes},
author = {Hagopian, W A and Tager, H S},
abstractNote = {A reverse-phase HPLC method has been developed to purify /sup 125/I-labeled products resulting from the chloramine-T-based iodination of glucagon. In addition the products ((/sup 125/I)iodoTyr/sup 10/ /sup 13/)glucagon, ((/sup 125/I)iodoTyr/sup 13/)glucagon, and ((/sup 125/I)iodoTyr/sup 10/)glucagon) have been used to study the receptor binding of glucagon and the cell-mediated metabolism of the hormone by isolated canine hepatocytes. It was concluded that (a) not withstanding apparent differences in affinities exhibited by the three peptides, the interactions with the glucagon receptor are functionally equivalent, and (b) the cell-mediated metabolism of receptor-bound glucagon involves the formation of hormone-derived peptides in which the biologically important NH/sub 2/-terminal region of the hormone has been modified by limited proteolytic cleavage.},
doi = {},
url = {https://www.osti.gov/biblio/5906365}, journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 259:14,
place = {United States},
year = {Wed Jul 25 00:00:00 EDT 1984},
month = {Wed Jul 25 00:00:00 EDT 1984}
}