Abstract
Transforming growth factors (TGF) are low molecular weight, acid-stable polypeptides that confer a malignant phenotype on nonneoplastic cells. TGF from murine sarcoma virus transformed 3T3 cells were isolated by acid/ethanol extraction, Bio-Gel P-30 chromatography, and reverse-phase high-performance liquid chromatography. Using a μBondapak C 18 column with an acetonitrile gradient, TGF activity can be resolved into two peaks, one of which requires epidermal growth factor (EGF) to induce colony formation of indicator cells in soft agar. Subsequent rechromatography of the EGF-dependent TGF on a μBondapak CN column using an n-propanol gradient resulted in a 430-fold purification over the acid/ethanol extract and showed soft agar activity at a concentration of 4 ng/ml in the presence of 2 ng/ml EGF. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed one main band with an apparent molecular weight of 13,000.
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