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Characterization of epidermal growth factor receptors on plasma membranes isolated from rat gastric mucosa

Journal Article · · Pharmaceutical Research; (USA)

The binding of human epidermal growth factor (hEGF), beta-urogastrone, to plasma membranes isolated from rat gastric mucosa was studied to characterize gastric EGF receptors. The binding of ({sup 125}I)hEGF was temperature dependent, reversible, and saturable. A single class of binding sites for EGF with a dissociation constant of 0.42 nM and maximal binding capacity of 42 fmol/mg protein was suggested. There was little change in the binding of ({sup 125}I)hEGF upon addition of peptide hormones (secretin, insulin), antiulcer drugs (cimetidine), or an ulcer-inducing reagent (aspirin). Cross-linking of ({sup 125}I)hEGF to gastric plasma membranes with the use of disuccinimidyl suberate resulted in the labeling of a protein of 150 kDa. These results indicate the presence of EGF receptors on plasma membranes of rat gastric mucosa.

OSTI ID:
6875205
Journal Information:
Pharmaceutical Research; (USA), Journal Name: Pharmaceutical Research; (USA) Vol. 7:6; ISSN 0724-8741; ISSN PHREE
Country of Publication:
United States
Language:
English