Selective cleavage of Arg- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme
Venombin A enzymes are the sole representatives of the defibrinogenating agent class of drugs, which by its protease action removes fibrinogen from the circulation. They are thought to act as an antithrombotic by depletion of fibrinogen.[6] They are different from thrombin in that they only cleave fibrinogen alpha chain (those do cleave both chains are called venombin AB), which will end up only producing weak, urea-soluble microthrombi that is easily removed by plasmin.[7] Their benefit in acute ischaemic stroke is not supported by available evidence.[8]
Alternatively, batroxobin is also used as a topical hemostatic by its rapid local clot-expansion action.[9]
^Simmons G, Bundalian M, Theodor I, Martinoli J, Pirkle H (November 1985). "Action of crotalase, an enzyme with thrombin-like and kallikrein-like specificities, on tripeptide nitroanilide derivatives". Thrombosis Research. 40 (4): 555–61. doi:10.1016/0049-3848(85)90292-0. PMID2934864.
^Kelton, JG; Smith, JW; Moffatt, D; Santos, A; Horsewood, P (1999). "The interaction of ancrod with human platelets". Platelets. 10 (1): 24–9. doi:10.1080/09537109976310. PMID16801067.
^Hao Z, Liu M, Counsell C, Wardlaw JM, Lin S, Zhao X (March 2012). "Fibrinogen depleting agents for acute ischaemic stroke". The Cochrane Database of Systematic Reviews (3): CD000091. doi:10.1002/14651858.CD000091.pub2. PMID22419274.
