| 摘要 |
<p>Purified mammalian thrombopoietin proteins and methods of making them are disclosed. The proteins are characterized by a Mr=70,000 ± 10,000 daltons as determined by SDS-polyacrylamide gel electrophoresis under denaturing conditions and are at least 90 % pure with respect to contaminating proteins. The proteins can be prepared by a method in which thrombopoietin is adsorbed to and eluted from a polypeptide comprising a ligand-binding domain of an MPL receptor, then the eluted thrombopoieting is fractionated by anion exchange chromatography.</p> |
