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- W1787673447 abstract "A latent form of transforming growth factor type-β (TGF-β) with a high molecular weight was purified to homogeneity from rat platelets by a six-step procedure. The yield of the purified latent TGF-β from platelets of 2, 500 rats was 1.4 mg. The purified latent TGF-β was activated by treatment with urea at concentrations of over 4M or acidic solutions of below pH 4. SDS-PAGE and gel filtration chromatography showed that the latent TGF-β consisted of active TGF-β and glycoproteins of about 200 kDa as masking components, and that under physiological conditions, these components formed a high molecular weight complex of about 400 kDa linked by non-covalent bonds. Here, we found that the masking protein was composed of one large subunit of about 110 kDa and two small subunits of 39 kDa linked by disulfide bridges. The N-terminal amino acid sequence of the small subunit was identical to the N-terminal region of the TGF-β precursor lacking a signal peptide. From these findings, we proposed a structural model for the latent TGF-β from rat platelets." @default.
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- W1787673447 date "1989-08-01" @default.
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- W1787673447 title "Purification and Structural Analysis of a Latent Form of Transforming Growth Factor-β from Rat Platelets1" @default.
- W1787673447 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a122849" @default.
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