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PMID: 3954725 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and partial sequence analysis of insulin-like growth factor-1 from bovine colostrum.

The Biochemical journal ·Vol. 233 ·No. 1 ·1986-01-01 ·Pages 207-13

Francis GL, Read LC, Ballard FJ, Bagley CJ, Upton FM, Gravestock PM, Wallace JC

Abstract

Growth-promoting activity in bovine colostrum has been detected as the capacity to stimulate protein synthesis in L6 myoblasts. By using this assay as a measure of bioactivity, a growth factor has been purified to near homogeneity from centrifuged colostrum by a series of steps including acid extraction, chromatography on sulphopropyl-Sephadex, followed by adsorption to, and elution from, C18 columns using acetonitrile and propan-1-ol gradients. The purified growth factor has a low solubility at neutral and alkaline pH and has an Mr of 7800 by gel-permeation chromatography. Sequence analysis of the first 30 amino acids from the N-terminus indicated complete identity in this region with human insulin-like growth factor-1. Accordingly we conclude that the purified growth factor is bovine insulin-like growth factor-1.

MeSH Terms
Amino Acid Sequence Animals Cattle Chromatography, Gel Chromatography, High Pressure Liquid Colostrum/analysis Female Insulin-Like Growth Factor I/isolation & purification Molecular Weight Pregnancy
Chemicals
Insulin-Like Growth Factor I
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Francis G L
Read L C
Ballard F J
Bagley C J
Upton F M
Gravestock P M
Wallace J C
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29 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2330207
Published
1986-01-01
Pages
207-13
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1153005
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2330207 PMC Full Text View journal details
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