Trypsin and chymotrypsin inhibitor peptides from the venom of Chinese Daboia russellii siamensis

Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

“…To date a number of BPTI-like superfamily serine protease inhibitors from Viperidae and Elapidae venoms have been purified or characterized [3,4,12,13,15,16,18,19,25,26,[29][30][31][32][33][34]35,36,39]. In this paper, one chymotrypsin inhibitor, BBPTI-1, was purified to homogeneity from the venom of Burmese Daboia russelli siamensis by gel filtration, cation exchange and reversed phase chromatography.…”

“…BBPTI-1 showed competitive chymotrypsin inhibitory activity, but no detectable trypsin inhibitory activity. Generally, chymotrypsin inhibitors exhibit no inhibitory trypsin activity, as is the case with Oh11-1 from Ophiophagus hannah venom [3], CBPTI-3 from Chinese Daboia russellii siamensis [13] and NA-CI from Naja atra venom [39], but Ritonja reported a chymotrypsin inhibitor that inhibited trypsin and human kallikrein weakly [31]. The Chinese Daoia russullii siamensis venom, 2.55nM [13], but lower than the reported value for Oh11-1 from Ophiophagus hannah venom, 3.52 µM [3] and NA-CI from Naja atra venom, 25 nM [39].…”

Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals

“…A Kunitz-type inhibitor homolog (RVV inhibitor II, UniProtKB P00990) was further sequenced from the venom of the Eastern Russel’s viper (= Daboia siamensis ) [115]. Recently, similar polypeptides were identified in the venom of Daboia siamensis [49,50]. From the Burmese specie, BBPTI-1 (Table 1) was shown to strongly inhibit chymotrypsin activity, with no detectable inhibitory activity against trypsin [49].…”

“…From the Burmese specie, BBPTI-1 (Table 1) was shown to strongly inhibit chymotrypsin activity, with no detectable inhibitory activity against trypsin [49]. From the Chinese one, two trypsin inhibitors (CBPTI-1 and CBPTI-2, Table 1) and one chymotrypsin inhibitor (CBPTI-3, Table 1) were purified and cloned [50]. …”

“…The P1 site residues Met, Asn and His for chymotrypsin binding were also reported [50,59,118,177,178]. A catalytic triad of residues (usually Ser, His and Asp) on the enzymes’ pocket is responsible for amide bond hydrolysis.…”