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

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Author

  • Hidenori Ichijo
  • Lars Rönnstrand
  • K Miyagawa
  • H Ohashi
  • Carl-Henrik Heldin
  • Kohei Miyazono

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.

Publishing year

1991

Language

English

Pages

22459-22464

Publication/Series

Journal of Biological Chemistry

Volume

266

Issue

33

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Medicinal Chemistry

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

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X