Purification of human platelet-derived growth factor.

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Abstract
Human platelets contain a polypeptide growth factor that stimulates the proliferation of connective tissue cells. Purification of this platelet-derived growth factor (PDGF) was accomplished by heat (100.degree. C) treatment of washed platelets and subsequent ion-exchange chromatography, gel filtration in 1 M acetic acid, isoelectric focusing and preparative sodium dodecyl sulfate/polyacrylamide gel electrophoresis. PDGF had an isoelectric point of 9.8 and a MW ranging from 13,000 to 16,000 as judged by gel filtration in 1 M acetic acid or analytical sodium dodecyl sulfate gel electrophoresis under reducing conditions. The specific activity of the purified PDGF was 20 million times greater than that found in unfractionated human serum. Purified PDGF stimulated replicative DNA synthesis and cell proliferation in quiescent density-arrested cultures of BALB/c [rat neoplastic fibroblasts] 3T3 cells at concentrations of 1 ng/ml (0.1 nM).