Purification, characterization and biological activities of phospholipase a from russell's viper (Vipera russelli) venom
Author:
Publisher
Elsevier BV
Subject
Biochemistry
Reference16 articles.
1. An indirect hemolytic assay for assessing antivenoms;Al-Abdulla;Toxicon,1991
2. Fractionation of Vipera russelli venom by gel nitration I;Dimitrov;Toxicon,1968
3. Isolation and pharmacological properties of phospholipase A2 from Vipera russelli Russell's viper snake venom;Huang;Toxicon,1984
4. Geographical variation in India in the composition and potency of Russell's viper (Vipera russelli) venom;Jayanthi;Toxicon,1988
5. Dissociation of catalytic activity and neurotoxicity of a basic phospholipase A2 from Russell's viper (Vipera russelli) venom;Jayanthi;Toxicon,1989
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2. Exploring the structural and functional aspects of the phospholipase A2 from Naja spp.;International Journal of Biological Macromolecules;2019-11
3. Quantitative proteomic analysis and antivenom study revealing that neurotoxic phospholipase A2 enzymes, the major toxin class of Russell's viper venom from southern India, shows the least immuno-recognition and neutralization by commercial polyvalent antivenom;International Journal of Biological Macromolecules;2018-10
4. Translational Venomics: Third-Generation Antivenomics of Anti-Siamese Russell’s Viper, Daboia siamensis, Antivenom Manufactured in Taiwan CDC’s Vaccine Center;Tropical Medicine and Infectious Disease;2018-06-15
5. An acidic phospholipase A2 (RVVA-PLA2-I) purified from Daboia russelli 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;Toxicon;2011-05
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