Purification of transforming growth factor-beta 1 binding proteins from porcine uterus membranes
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1784213
- author
- Ichijo, Hidenori ; Rönnstrand, Lars LU ; Miyagawa, K ; Ohashi, H ; Heldin, Carl-Henrik and Miyazono, Kohei
- publishing date
- 1991
- 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}}, }