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

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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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
Volume108
Issue number1
DOIs
StatePublished - Sep 16 1982
Externally publishedYes

Fingerprint

Isoelectric Focusing
Epidermal Growth Factor
Processing
Halogenation
Isoelectric Point
Molecules
Fibroblasts
Macromolecules
Rats
Sodium
High Pressure Liquid Chromatography

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Binding, internalization and intracellular processing of 125I-epidermal growth factor purified by isoelectric focusing. / Magun, Bruce E.; Planck, Stephen; Matrisian, Lynn M.; Finch, Joanne S.

In: Biochemical and Biophysical Research Communications, Vol. 108, No. 1, 16.09.1982, p. 299-306.

Research output: Contribution to journalArticle

@article{ece64d2d5284400c9f78f92be7432e95,
title = "Binding, internalization and intracellular processing of 125I-epidermal growth factor purified by isoelectric focusing",
abstract = "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.",
author = "Magun, {Bruce E.} and Stephen Planck and Matrisian, {Lynn M.} and Finch, {Joanne S.}",
year = "1982",
month = "9",
day = "16",
doi = "10.1016/0006-291X(82)91866-6",
language = "English (US)",
volume = "108",
pages = "299--306",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Binding, internalization and intracellular processing of 125I-epidermal growth factor purified by isoelectric focusing

AU - Magun, Bruce E.

AU - Planck, Stephen

AU - Matrisian, Lynn M.

AU - Finch, Joanne S.

PY - 1982/9/16

Y1 - 1982/9/16

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0020420083&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020420083&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(82)91866-6

DO - 10.1016/0006-291X(82)91866-6

M3 - Article

C2 - 6293485

AN - SCOPUS:0020420083

VL - 108

SP - 299

EP - 306

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -