Human platelet-derived growth factor. Purification and resolution into two active protein fractions

T F Deuel, J S Huang, R T Proffitt, J U Baenziger, D Chang, B B Kennedy
1981 Journal of Biological Chemistry  
Human platelets secrete a factor that stimulates cultured human cells to initiate DNA synthesis and to divide. This human platelet-derived growth factor (PDGF) has been purified congruent to 100,000-fold into two equally active homogeneous fractions, PDGF I (Mr congruent to 31,000) and PDGF II (Mr congruent to 28,000). The amino acid compositions of each are similar, highly basic, and show 18 half-cystine residues. Both PDGF I and II are glycoproteins, but differ in their carbohydrate
more » ... ns. The data suggest that PDGF II may be a proteolytic cleavage product of PDGF I but do not rule out that the proteins may be separate but very similar gene products. Purified PDGF is active in stimulating DNA synthesis at 0.2 ng/ml.
pmid:7263691 fatcat:lvdhf5g6arflfkxc5u5ik2geqq