Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

J. C. Byatt, B. R. Larson, M. P. Baganoff, M. F. McGrath, Robert J Collier

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.

Original languageEnglish (US)
Pages (from-to)1179-1187
Number of pages9
JournalBiochemistry International
Volume20
Issue number6
StatePublished - 1990
Externally publishedYes

Fingerprint

Epidermal Growth Factor
Purification
Radioligand Assay
Transforming Growth Factor alpha
Peptides
Assays
Intercellular Signaling Peptides and Proteins
Breast
Epithelial Cells
Kidney
Amino Acids
Molecules
Chemical analysis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification and partial characterization of a bovine epidermal growth factor-like polupeptide. / Byatt, J. C.; Larson, B. R.; Baganoff, M. P.; McGrath, M. F.; Collier, Robert J.

In: Biochemistry International, Vol. 20, No. 6, 1990, p. 1179-1187.

Research output: Contribution to journalArticle

Byatt, JC, Larson, BR, Baganoff, MP, McGrath, MF & Collier, RJ 1990, 'Purification and partial characterization of a bovine epidermal growth factor-like polupeptide', Biochemistry International, vol. 20, no. 6, pp. 1179-1187.
Byatt, J. C. ; Larson, B. R. ; Baganoff, M. P. ; McGrath, M. F. ; Collier, Robert J. / Purification and partial characterization of a bovine epidermal growth factor-like polupeptide. In: Biochemistry International. 1990 ; Vol. 20, No. 6. pp. 1179-1187.
@article{1ba4f08a220b41e0ae808b4c660e9110,
title = "Purification and partial characterization of a bovine epidermal growth factor-like polupeptide",
abstract = "A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.",
author = "Byatt, {J. C.} and Larson, {B. R.} and Baganoff, {M. P.} and McGrath, {M. F.} and Collier, {Robert J}",
year = "1990",
language = "English (US)",
volume = "20",
pages = "1179--1187",
journal = "IUBMB Life",
issn = "1521-6543",
publisher = "Wiley-Blackwell",
number = "6",

}

TY - JOUR

T1 - Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

AU - Byatt, J. C.

AU - Larson, B. R.

AU - Baganoff, M. P.

AU - McGrath, M. F.

AU - Collier, Robert J

PY - 1990

Y1 - 1990

N2 - A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.

AB - A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.

UR - http://www.scopus.com/inward/record.url?scp=0025293023&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025293023&partnerID=8YFLogxK

M3 - Article

C2 - 2369415

AN - SCOPUS:0025293023

VL - 20

SP - 1179

EP - 1187

JO - IUBMB Life

JF - IUBMB Life

SN - 1521-6543

IS - 6

ER -