title: Partial purification and characterization of porcine platelet-derived growth factor (PDGF).
abstract: Platelet derived growth factor (PDGF) has been partially purified from porcine platelets. Purification steps included heparin-agarose chromatography of the material released by thrombin-stimulated washed porcine platelets and Blue-Sepharose chromatography. Preparative isoelectric focusing showed that isoelectric point of porcine PDGF is at pH 10.0-11.0 and elution experiments from sodium dodecyl sulfate (SDS) polyacrylamide gels indicated that its molecular weight is close to 30 kD. The immunoglobulin fraction prepared from anti-human PDGF serum inhibited the mitogenic activity of porcine PDGF. These experiments suggest a homology of porcine and human PDGF. Porcine platelet factor 4 and porcine platelet basic protein were devoid of significant mitogenic activity.
mesh_terms: D000818:Animals; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007526:Isoelectric Point; D008970:Molecular Weight; D010982:Platelet-Derived Growth Factor / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D013552:Swine / Q000097:blood*
chemical_list: D010982:Platelet-Derived Growth Factor