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.
MeSH terms
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Animals
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Carrier Proteins / isolation & purification*
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Carrier Proteins / metabolism
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Cell Membrane / metabolism
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Chromatography, Affinity
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Female
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Intracellular Signaling Peptides and Proteins*
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Latent TGF-beta Binding Proteins
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Membrane Glycoproteins / isolation & purification*
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Membrane Glycoproteins / metabolism
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Molecular Weight
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Platelet-Derived Growth Factor / metabolism
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Receptors, Cell Surface / isolation & purification
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Receptors, Cell Surface / metabolism
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Receptors, Platelet-Derived Growth Factor
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Recombinant Proteins / metabolism
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Swine
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Transforming Growth Factor beta / metabolism*
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Uterus / metabolism*
Substances
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Carrier Proteins
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Intracellular Signaling Peptides and Proteins
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Latent TGF-beta Binding Proteins
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Membrane Glycoproteins
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Platelet-Derived Growth Factor
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Receptors, Cell Surface
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Recombinant Proteins
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Transforming Growth Factor beta
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Receptors, Platelet-Derived Growth Factor