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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.
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
January 1989,
Archivum immunologiae et therapiae experimentalis,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
October 1986,
Cancer research,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
January 1987,
Methods in enzymology,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
September 1986,
Journal of biochemistry,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
February 1992,
The Journal of biological chemistry,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
June 1983,
Proceedings of the National Academy of Sciences of the United States of America,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
January 1988,
Analytical biochemistry,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
November 1996,
Die Pharmazie,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
October 1996,
Biology of reproduction,
A B Roberts, and
M A Anzano, and
C A Meyers, and
J Wideman, and
R Blacher, and
Y C Pan, and
S Stein, and
S R Lehrman, and
J M Smith, and
L C Lamb
February 1990,
Journal of cellular biochemistry,
