OBJECTIVE To investigate the expression efficiency of human platelet-derived growth factor B-chain (PDGF-B) gene in yeast and assess the activity of the expressed product. METHODS A full-length complementary DNA of human PDGF-B gene was amplified from the total RNA extracted from human vascular endothelial cells using reverse transcription (RT)-PCR and then cloned into pGEM-T vector. The PCR products with specific primers were recombined into yeast expression plasmids pMETB or pMETalphaA, followed by identification with restriction endonuclease. RESULTS The 578 bp fragment encoding mature PDGF-BB peptide with signal peptide and the 340 bp fragment without signal peptide were identified and verified by restriction endonuclease mapping and sequencing, and two yeast expression vectors pMETB-PDGFB(1) and pMETalphaA-PDGFB(2) were reconstructed. CONCLUSIONS The yeast expression vectors containing human PDGF-B gene have been successfully constructed for further studies of gene expression in yeast.