Objective    To fulfill high-efficient expression of rTMP-GH

a recombinant fusion protein of thrombopoietin mimetic peptide and human growth hormone

in Pichia pastoris.     Methods    cDNA fragment coding for rTMP-GH was amplified by PCR

and subsequently cloned into the expression vector pPIC9K. The linearlized plasmid pPIC9K-rTMP-GH was transformed into Pichia pastoris GS115 cells and screened in MD/MM plates under pressure of G418. The recombinant fusion protein rTMP-GH was identified by Western blotting

and its biological activity was analyzed by its ability on colony formation of megakaryoblasts.     Results    The pPIC9K-rTMP-GH expression plasmid was successfully constructed. GS115 cells with high expression of rTMP-GH was screened out

and the rough purified rTMP-GH showed promotive effect on megakaryoblast colony formation.     Conclusion    High-efficient expression of rTMP-GH in Pichia pastoris is achieved.