A new C-type lectin (RVsnaclec) purified from venom of Daboia russelii russelii shows anticoagulant activity via inhibition of FXa and concentration-dependent differential response to platelets in a Ca2+-independent manner
Author:
Publisher
Elsevier BV
Subject
Hematology
Reference26 articles.
1. Some biochemical properties of Russell’s viper (Daboia russelli) venom from Eastern India: correlation with clinic-pathological manifestation in Russell’s viper bite;Mukherjee;Toxicon,2000
2. An acidic phospholipase A2 (RVVA-PLA2-I) purified from Daboia russelii venom exerts its anticoagulant activity by enzymatic hydrolysis of plasma phospholipids and by non-enzymatic inhibition of factor Xa in a phospholipids/Ca2+ independent manner;Saikia;Toxicon,2011
3. Biochemical and pharmacological properties of a new thrombin-like serine protease (Russelobin) from the venom of Russell’s viper (Daboia russelii russelii) and assessment of its therapeutic potential;Mukherjee;Biochim Biophys Acta,2013
4. The pro-coagulant fibrinogenolytic serine protease isoenzymes from Daboia russelii russelii venom coagulate the blood through factor V activation: Role of glycosylation on enzymatic activity;Mukherjee;PLoS One,2014
5. A major phospholipase A2 from Daboia russelli russelii venom shows potent anticoagulant action via thrombin inhibition and binding with plasma phospholipids;Mukherjee;Biochimie,2014
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