Purification,characterization and biological activities of phospholipase a from russell's viper (Vipera russelli) venom |
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| Institution: | 1. Department of Medical Research, No. 5, Ziwaka Road, Dagon P.O., Yangon, MyanmarBurma;2. Biochemistry Department, Institute of Medicine, Mandalay, Myanmar, Burma;1. Facultad de Ciencias Biológicas, Universidad Juárez del Estado de Durango, Av. Universidad s/n. Fracc. Filadelfia, C.P. 35010, Gómez Palacio, Dgo., Mexico;2. Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Chamilpa, C.P. 62210, Cuernavaca, Mor., Mexico;3. Department of Biology, University of South Alabama, 5871 USA Dr. N., Mobile, AL, 36688, USA;4. Department of Biological Sciences, Clemson University, Clemson, SC, 29634, USA;1. Laboratory of Toxinology and Cardiovascular Research, Graduate Program in Health Sciences, University of Western São Paulo (UNOESTE), Presidente Prudente, SP, Brazil;2. Laboratory of Pathological Anatomy, Veterinary Hospital, University of Western São Paulo (UNOESTE), Presidente Prudente, SP, Brazil;3. Laboratory of Herpetology, Butantan Institute (IB), São Paulo, SP, Brazil;4. Section of Pharmacology, Department of Translational Medicine, Faculty of Medical Sciences, State University of Campinas (UNICAMP), Campinas, SP, Brazil |
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| Abstract: | - 1.1. The major phospholipase A has been purified to electrophoretic homogeneity from the venom of Vipera russelli (Russell's viper).
- 2.2. The molecular weight of the purified enzyme was estimated to be 31,000 by Sephadex G-75 gel filtration chromatography and 29,000 by SDS-polyacrylamide gel electrophoresis. The enzyme exhibited an apparent Km value of 2.3 × 10?2 M.
- 3.3. The phospholipase A showed edema forming, indirect hemolytic and myonecrotic activities but not hemorrhagic activity.
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