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Purification and properties of a type .beta. transforming growth factor from bovine kidney
Abstract
Type beta transforming growth factor (TGF-beta) has been purified 200 000-fold from bovine kidneys. This peptide is characterized by its ability to induce anchorage-dependent normal rat kidney cells to grow in soft agar in the presence of epidermal growth factor (EGF); TGF-beta is not mitogenic for cells grown in monolayer culture. Purified TGF-beta does not compete with EGF for binding to membrane receptors. The concentration of TGF-beta required to elicit a half-maximal response for formation of colonies greater than 3100 micron2 in the soft agar assay is 2-3 pM (55 pg/mL) when assayed in the presence of 0.8 nM EGF (5 ng/mL). The four-step purification procedure which includes chromatography of acid--ethanol tissue extracts on polyacrylamide sizing gels, cation exchange, and two steps of high-pressure liquid chromatography results in a 10% overall yield of colony-forming activity with a recovery of 3-4 micrograms/kg. Amino acid analysis of purified TGF-beta shows 16 half-cystine residues per mole. Analysis of the purified polypeptide by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels indicates that TGF-beta is composed of two closely related polypeptide chains cross-linked by disulfide bonds. In the absence of beta-mercaptoethanol, the colony-forming activity is associated with a single silver-staining band of molecular weight 25 000; in the presence of beta-mercaptoethanol, the TGF-beta is converted to an inactive species that migrates as a single band of molecular weight 12 500-13 000. Sequence analysis indicates that at least the first 15 N-terminal amino acids of the two TGF-beta subunits are identical.
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Citations
Cited by
Ignotz, R. A., & Massagué, J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35666-1 · Cited by 2,492
TGF-β and the TGF-β family: context-dependent roles in cell and tissue physiology
Morikawa, M., Derynck, R., & Miyazono, K. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021873 · Cited by 1,321
Edwards, D. R., Murphy, G., Reynolds, J. J., Whitham, S. E., Docherty, A. J., Angel, P., & Heath, J. K. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02449.x · Cited by 1,221
Transforming Growth Factor‐β: Major Role in Regulation of Extracellular Matrix
ROBERTS, A. B., HEINE, U. I., FLANDERS, K. C., & SPORN, M. B. (1990) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1990.tb17931.x · Cited by 696
Self-citationTGF-β signaling in vascular biology and dysfunction
Goumans, M.-J., Liu, Z., & ten Dijke, P. (2009) · Cell Research · doi:10.1038/cr.2008.326 · Cited by 601
Metadata
- Authors
- Roberts, A. B., Anzano, M. A., Meyers, C. A., Wideman, J., Blacher, R., Pan, Y. C. E., Stein, S., Lehrman, S. R., & Smith, J. M.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1983-12-01
- Volume
- 22
- Issue
- 25
- Pages
- 5692-5698
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2041149723
- Cited by
- 352
- References
- 0
- FWCI
- 11.65
- Type
- journal article
- Language
- en
- Open access
- closed
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- Roberts, A. B., Anzano, M. A., Meyers, C. A., Wideman, J., Blacher, R., Pan, Y. C. E., Stein, S., Lehrman, S. R., & Smith, J. M. (1983). Purification and properties of a type .beta. transforming growth factor from bovine kidney. Biochemistry. https://doi.org/10.1021/bi00294a002
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