The present study describes the purification and partial characterization of a basic anticoagulant PLA enzyme named as Rv(i) PLA from the venom of Indian Daboia russelii. The molecular mass of the protein was found to be 13,659.65 Da, and peptide mass fingerprinting revealed that it belongs to group II PLA family. The peptide sequence showed similarity to uncharacterized basic PLA enzyme having an accession no. of P86368 reported from Sri Lankan D. russelii. Rv(i) PLA exhibited strong phospholipase A and anticoagulant activity. It also induced expression of COX-2 and TNF-α mRNA in a dose-dependent manner in phorbol 12-myristate 13-acetate differentiated THP-1 cells, which play a crucial role during inflammation. Chemical modification of His residue in Rv(i) PLA with p-bromophenacyl bromide abolished the enzymatic, anticoagulant, and inflammatory activities. The result indicates that the catalytic site of Rv(i) PLA might play a vital role in inducing inflammation at the bite site during D. russelii envenomation.