One　novel　Kunitz　BPTI-like　peptide　designated　as　BBPTI-1,　with　chymotrypsin　inhibitory　activity　was　identified　from　the　venom　of　Burmese　Daboia　russelii　siamensis.　It　was　purified　by　three　steps　of　chromatography　including　gel　filtration,　cation　exchange　and　reversed　phase.　A　partial　N-terminal　sequence　of　BBPTI-1,　HDRPKFCYLPADPGECLAHMRSF　was　obtained　by　automated　Edman　degradation　and　a　Ki　value　of　4.77　nM　determined.　Cloning　of　BBPTI-1　including　the　open　reading　frame　and　3＇　untranslated　region　was　achieved　from　cDNA　libraries　derived　from　lyophilized　venom　using　a　3＇　RACE　strategy.　In　addition　a　cDNA　sequence,　designated　as　BBPTI-5,　was　also　obtained.　Alignment　of　cDNA　sequences　showed　that　BBPTI-5　exhibited　an　identical　sequence　to　BBPTI-1　cDNA　except　for　an　eight　nucleotide　deletion　in　the　open　reading　frame.　Gene　variations　that　represented　deletions　in　the　BBPTI-5　cDNA　resulted　in　a　novel　protease　inhibitor　analog.　Amino　acid　sequence　alignment　revealed　that　deduced　peptides　derived　from　cloning　of　their　respective　precursor　cDNAs　from　libraries　showed　high　similarity　and　homology　with　other　Kunitz　BPTI　proteinase　inhibitors.　BBPTI-1　and　BBPTI-5　consist　of　60　and　66　amino　acid　residues　respectively,　including　six　conserved　cysteine　residues.　As　these　peptides　have　been　reported　to　have　influence　on　the　processes　of　coagulation,　fibrinolysis　and　inflammation,　their　potential　application　in　biomedical　contexts　warrants　further　investigation.　(C)　2013　Elsevier　Inc.　All　rights　reserved.