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

Research output: Contribution to journalArticle

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.

Details

Authors
  • Hidenori Ichijo
  • Lars Rönnstrand
  • K Miyagawa
  • H Ohashi
  • Carl-Henrik Heldin
  • Kohei Miyazono
External organisations
  • Ludwig Institute for Cancer Research, Uppsala branch
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • 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
Original languageEnglish
Pages (from-to)22459-22464
JournalJournal of Biological Chemistry
Volume266
Issue number33
Publication statusPublished - 1991
Publication categoryResearch
Peer-reviewedYes
Externally publishedYes

Bibliographic note

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)