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

doi:10.1016/0006-291X(82)91866-6

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 journal › Article › peer-review

12 Scopus citations

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 language	English (US)
Pages (from-to)	299-306
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	108
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(82)91866-6
State	Published - Sep 16 1982

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

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

Cite this

@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 Planck, {Stephen R.} and Matrisian, {Lynn M.} and Finch, {Joanne S.}",

note = "Funding Information: This work is supported",

year = "1982",

month = sep,

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 R.

AU - Matrisian, Lynn M.

AU - Finch, Joanne S.

N1 - Funding Information: This work is supported

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

SN - 0006-291X

VL - 108

SP - 299

EP - 306

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this