Objective To clone the prokaryotic expression of leptin mature peptide and a partial leptin receptor extracellular domain in Tibet minipig． Methods Two pairs of primers，amplifying the 64 － 504 bp leptin mature peptide coding region，and 1654 － 2319 bp leptin receptor ( OBR) extracellular domain ( ECD) ，were designed and synthesized according to the sequences of swine leptin ( GenBank No． GQ240885. 1) and OBR ( GenBank No． AF167719. 1) genes． Total RNA was extracted from the Tibet minipig liver tissue，and was used as the template in RT-PCR to amplify the cDNA fragments coding leptin mature peptide and OBR ECD． The two fragments were then cloned into the pMD18 -T vector and the resultant plasmid was transformed into competent E． coli strain DH5α． The fragments were digested and cloned into the BamHⅠand HindⅢ sites of the expression vector pRSETA to form the recombinant plasmids pR-OB and pR-OBR-a，which were subsequently transformed into E． coli strain BL21 ( DE3 ) for expression of the recombinant proteins． Results The transformed bacteria pR-OB and pR-OBR-a were induced with IPTG and produced recombinant proteins of the relative molecular mass of 17. 5 × 103 and 27 × 103，respectively． Conclusions pR-OB and pR-OBR-a can express recombinant porcine leptin mature peptide and a partial OBR ECD of Tibet minipig in E． coli． strain BL21( DE3) ． This work provided the basis for further research on pig leptin and OBR．