Purification of transforming growth factor-beta 1 binding proteins from porcine uterus membranes
Författare
Summary, in English
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.
Publiceringsår
1991
Språk
Engelska
Sidor
22459-22464
Publikation/Tidskrift/Serie
Journal of Biological Chemistry
Volym
266
Issue
33
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Biochemistry and Molecular Biology
Ämne
- Medicinal Chemistry
Nyckelord
- 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
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1083-351X