猪血小板衍生生长因子（PDGF）的部分纯化及特性分析

Partial purification and characterization of porcine platelet-derived growth factor (PDGF).

作者信息

Poggi A, Rucinski B, James P, Holt J C, Niewiarowski S

出版信息

Exp Cell Res. 1984 Feb;150(2):436-41. doi: 10.1016/0014-4827(84)90587-1.

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.

摘要

血小板衍生生长因子（PDGF）已从猪血小板中部分纯化。纯化步骤包括对凝血酶刺激的洗涤过的猪血小板释放的物质进行肝素 - 琼脂糖层析和蓝色琼脂糖层析。制备性等电聚焦显示猪PDGF的等电点在pH 10.0 - 11.0，并且从十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶上的洗脱实验表明其分子量接近30 kD。从抗人PDGF血清制备的免疫球蛋白组分抑制了猪PDGF的促有丝分裂活性。这些实验表明猪和人PDGF具有同源性。猪血小板因子4和猪血小板碱性蛋白没有显著的促有丝分裂活性。