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. 1979 Aug;76(8):3722-6.
doi: 10.1073/pnas.76.8.3722.

Platelet-derived growth factor: purification and partial characterization

C H Heldin, B Westermark, A Wasteson

Platelet-derived growth factor: purification and partial characterization

C H Heldin et al. Proc Natl Acad Sci U S A. 1979 Aug.

Abstract

A cationic protein that stimulates DNA synthesis in human cultured cells was isolated from human platelets by ion exchange chromatography, hydrophobic chromatography, gel chromatography, and gel electrophoresis in sodium dodecyl sulfate. The electrophoretic behavior of biologically active or radioiodinated and reduced growth factor indicated that the native protein (approximately 30,000 daltons) was composed of two different polypeptides (approximately 13,000-14,000 and 16,000-17,000 daltons, respectively) linked via reduction-susceptible bonds. The stimulatory activity on human glial cells of the purified product at a concentration of approximately 4 ng/ml (0.13 nM) was equal to that of 1% human serum.

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