Snake venom phospholipase A2 (PLA2). In vitro, shows anticoagulant activity and induces cytotoxicity when tested on C2C12 myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity (intramuscular injection), edema (injection in the subplantar region) and lethality. Also induces neurotoxic effect on mouse neuromuscular preparations and has bactericidal activity on the Gram-negative bacteria E.coli (ATCC29648) and the Gram-positive S.aureus (ATCC 25923). The catalytic and anticoagulant activities of BnpTX-I are higher than those of BnpTX-II. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) Binds 1 Ca(2+) ion. P-bromophenacyl bromide (BPB) completely inhibit the catalytic activity whereas it only partially reduces the toxic activities. EDTA and magnesium ions partially inhibit the catalytic activity and partially reduce the toxic activities. Dimer. Expressed by the venom gland. Contains 7 disulfide bonds. LD(50) is 5.1 +/- 1.3 mg/kg by intraperitoneal injection into mice. LD(50) is 2.3 +/- 0.8 mg/kg by intravenous injection into mice. Has a pI of approximately 7.8 and about 121 amino acids. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.