Snake venom phospholipase A2 (PLA2) that shows a moderate inhibition of ADP-induced human platelet aggregation when tested on platelet rich plasma. Exhibits high hydrolytic activities and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). 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. Expressed by the venom gland. Is expressed more abundantly in juvenile than in adult vipers. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily. According to PubMed:12959640, T.stejnegeri was formerly named T.gramineus, supposing that this protein is the same as PLA-I from T.gramineus. They have been kept separated, because T.gramineus and T.stejnegeri are considered as being two different species (see http://reptile-database.org).