Platelet-derived growth factor: purification and partial characterization.
Proceedings of the National Academy of SciencesPublished 1 August 1979Open access
Carl‐Henrik Heldin, Bengt Westermark, Åke Wasteson
Citations434
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TL;DR
The electrophoretic behavior of biologically active or radioiodinated and reduced growth factor indicated that the native protein was composed of two different polypeptides linked via reduction-susceptible bonds.
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.
Keywords
Biochemistry, Genetics and Molecular Biology
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