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Purification of transforming growth factor-beta 1 binding proteins from porcine uterus membranes

Ichijo, Hidenori ; Rönnstrand, Lars LU orcid ; Miyagawa, K ; Ohashi, H ; Heldin, Carl-Henrik and Miyazono, Kohei (1991) In Journal of Biological Chemistry 266(33). p.22459-22464
Abstract
We have identified several transforming growth factor-beta 1 (TGF-beta 1) binding proteins in solubilized and glycoprotein-enriched porcine uterus membrane fractions by affinity cross-linking and in-gel ligand binding using 125I-labeled TGF-beta 1. By a ligand affinity chromatography using a column of immobilized recombinant TGF-beta 1, four components of apparent molecular weights 160,000, 80,000, 50,000, and 40,000 under reducing conditions were eluted at a pH of 3.5; the 160-,80-, and 40-kDa components were demonstrated to bind TGF-beta 1 specifically by the 125I-TGF-beta 1 binding assays. Further purification was performed by gel chromatography using a Superose 12 column eluted in 70% formic acid. The 40-kDa component was purified to... (More)
We have identified several transforming growth factor-beta 1 (TGF-beta 1) binding proteins in solubilized and glycoprotein-enriched porcine uterus membrane fractions by affinity cross-linking and in-gel ligand binding using 125I-labeled TGF-beta 1. By a ligand affinity chromatography using a column of immobilized recombinant TGF-beta 1, four components of apparent molecular weights 160,000, 80,000, 50,000, and 40,000 under reducing conditions were eluted at a pH of 3.5; the 160-,80-, and 40-kDa components were demonstrated to bind TGF-beta 1 specifically by the 125I-TGF-beta 1 binding assays. Further purification was performed by gel chromatography using a Superose 12 column eluted in 70% formic acid. The 40-kDa component was purified to an apparently homogenous form, whereas the 160-kDa component eluted in a broad peak overlapping the peak of the 80-kDa component. It remains to be elucidated whether these TGF-beta 1 binding proteins are related to cell surface receptors for TGF-beta s. (Less)
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publishing date
type
Contribution to journal
publication status
published
subject
keywords
Cell Surface/isolation & purification/metabolismReceptors, GelChromatography, High Pressure LiquidChromatography, Ion ExchangeElectrophoresis, Polyacrylamide GelFemale*Intracellular Signaling Peptides and ProteinsLatent TGF-beta Binding ProteinsMembrane Glycoproteins/*isolation & purification/metabolismMolecular WeightPlatelet-Derived Growth Factor/metabolismReceptors, AffinityChromatography, AnimalsCarrier Proteins/*isolation & purification/metabolismCell Membrane/metabolismChromatography, Platelet-Derived Growth FactorRecombinant Proteins/metabolismSwineTransforming Growth Factor beta/*metabolismUterus/*metabolism
in
Journal of Biological Chemistry
volume
266
issue
33
pages
22459 - 22464
publisher
American Society for Biochemistry and Molecular Biology
ISSN
1083-351X
language
English
LU publication?
no
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
id
07dd3f7d-6fba-4996-9f68-0475d36db502 (old id 1784213)
alternative location
http://www.jbc.org/content/266/33/22459.abstract
date added to LUP
2016-04-04 07:30:48
date last changed
2020-05-26 15:13:11
@article{07dd3f7d-6fba-4996-9f68-0475d36db502,
  abstract     = {{We have identified several transforming growth factor-beta 1 (TGF-beta 1) binding proteins in solubilized and glycoprotein-enriched porcine uterus membrane fractions by affinity cross-linking and in-gel ligand binding using 125I-labeled TGF-beta 1. By a ligand affinity chromatography using a column of immobilized recombinant TGF-beta 1, four components of apparent molecular weights 160,000, 80,000, 50,000, and 40,000 under reducing conditions were eluted at a pH of 3.5; the 160-,80-, and 40-kDa components were demonstrated to bind TGF-beta 1 specifically by the 125I-TGF-beta 1 binding assays. Further purification was performed by gel chromatography using a Superose 12 column eluted in 70% formic acid. The 40-kDa component was purified to an apparently homogenous form, whereas the 160-kDa component eluted in a broad peak overlapping the peak of the 80-kDa component. It remains to be elucidated whether these TGF-beta 1 binding proteins are related to cell surface receptors for TGF-beta s.}},
  author       = {{Ichijo, Hidenori and Rönnstrand, Lars and Miyagawa, K and Ohashi, H and Heldin, Carl-Henrik and Miyazono, Kohei}},
  issn         = {{1083-351X}},
  keywords     = {{Cell Surface/isolation & purification/metabolismReceptors; GelChromatography; High Pressure LiquidChromatography; Ion ExchangeElectrophoresis; Polyacrylamide GelFemale*Intracellular Signaling Peptides and ProteinsLatent TGF-beta Binding ProteinsMembrane Glycoproteins/*isolation & purification/metabolismMolecular WeightPlatelet-Derived Growth Factor/metabolismReceptors; AffinityChromatography; AnimalsCarrier Proteins/*isolation & purification/metabolismCell Membrane/metabolismChromatography; Platelet-Derived Growth FactorRecombinant Proteins/metabolismSwineTransforming Growth Factor beta/*metabolismUterus/*metabolism}},
  language     = {{eng}},
  number       = {{33}},
  pages        = {{22459--22464}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Purification of transforming growth factor-beta 1 binding proteins from porcine uterus membranes}},
  url          = {{http://www.jbc.org/content/266/33/22459.abstract}},
  volume       = {{266}},
  year         = {{1991}},
}