Abstract: Porcine bactericidal/permeability increasing protein (BPI) gene was cloned from porcine blood by reverse transcriptionpolymerase chain reaction (RTPCR). Sequence analysis showed that the porcine BPI cDNA cloned was 1 874 bp in length (GenBank accession No: FJ810853)and the open reading frame encoded 483 amino acids residues including 13.25% leucines and a signal peptide of 27 amino acids. Comparison analysis showed that homology of BPI amino acids sequence between porcine and that of human, cattle, rabbit, dog, rat, mouse, carp, xenopus laevis, atlantic salmon and large yellow croaker were 64%,74%, 59%, 67%, 53%, 51%, 35%, 44%, 28% and 27%, respectively. The amino terminal and the carboxyl terminal were two distinct functional domains, and an ultra-active domain was contained in each of the terminals and between the two terminals there existed trypsin hydrolytic site, which was the common structural features of human’s BPI.