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Receptor-purified, Bolton-Hunter radioiodinated, recombinant, human epidermal growth factor: An improved radioligand for receptor studies

Journal Article · · Journal of Receptor Research; (USA)
OSTI ID:6532389
;  [1]
  1. Univ. of Vermont College of Medicine, Burlington (USA)
We report an assessment of the applicability of the Bolton-Hunter method to the radioiodination of epidermal growth factor (EGF). Recombinant human EGF (hEGF) could be radioiodinated successfully by this method, whereas murine EGF could not. Bolton-Hunter {sup 125}I-labeled hEGF was compared with commercial 125I-labeled hEGF prepared by the chloramine-T radioiodination method. Neither radioligand was sufficiently pure for a detailed characterization of the purportedly heterogeneous pattern of binding of EGF to its receptors. A procedure based on receptor adsorption was thus developed for repurification of the Bolton-Hunter 125I-labeled hEGF. This provided a much purer radioligand suitable for detailed studies of receptor-binding heterogeneity.
OSTI ID:
6532389
Journal Information:
Journal of Receptor Research; (USA), Journal Name: Journal of Receptor Research; (USA) Vol. 9:6; ISSN 0197-5110; ISSN JRERD
Country of Publication:
United States
Language:
English