Receptor binding and cell-mediated metabolism of (/sup 125/I)monoiodoglucagon by isolated canine hepatocytes
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.
- Research Organization:
- Univ. of Chicago, IL
- OSTI ID:
- 5906365
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 259:14
- Country of Publication:
- United States
- Language:
- English
Similar Records
Receptor-linked degradation of /sup 125/I-insulin is mediated by internalization in isolated rat hepatocytes
Dynamic determination of kinetic parameters for the interaction between polypeptide hormones and cell-surface receptors in the perfused rat liver by the multiple-indicator dilution method
Related Subjects
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