Binding, internalization and intracellular processing of 125I-epidermal growth factor purified by isoelectric focusing

Bruce E. Magun, Stephen R. Planck, Lynn M. Matrisian, Joanne S. Finch

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


When epidermal growth factor (EGF) which had been extensively purified by HPLC was subjected to iodination with sodium 125iodide, 5 major species of differing isoelectric points were produced. Some of these species bound to rat fibroblasts with different affinities but were internalized with equal efficiency. Examination of the internalized 125I-labelled molecules revealed processing of all the 125I-EGF species to macromolecules with more acidic isoelectric points. The 125I-EGF species with a pI of 4.5 corresponded in electrofocusing behavior with intact non-iodinated EGF. Other EGF species probably represented molecules which were covalently modified as a result of the iodination procedure.

Original languageEnglish (US)
Pages (from-to)299-306
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Sep 16 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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