title: Isolation and characterization of biologically active venom protein from sea snake Enhydrina schistosa.
abstract: The present study is designed to investigate the isolation and characterization of biological and biochemical active venom protein from sea snake, Enhydrina schistosa. The highest purification peaks in ion-exchange chromatography on DEAE-cellulose column were obtained for fraction numbers 39-49 when eluted with 0.35-0.45 M NaCl. Eighty per cent purity was obtained in the final stage of purification, and a single protein band of about 44 kDa was visualized in SDS-polyacrylamide gel under reducing condition. Purified venom protein expressed as haemolytic, cytotoxicity and proteolytic activities with lethal concentration (LC50 ) at 2.0 μg/mL. Venom protein exhibits enzymatic activity and hydrolyzed casein and gelatin. Gelatinolytic activity was optimal at pH 5-9. In conclusion, the present results suggested that the sea snake venom might be feasible sources for biologically active substances. Thus, this low molecular weight component of the venom protein could be used in potentially serve biological and pharmaceutical aspects.
authors.affiliation: Centre of Advanced Study in Marine Biology, Faculty of Marine Sciences, Annamalai University, Parangipettai, 608 502, India. damotharanp@gmail.com.
authors.forename: Palani
authors.initials: P
authors.lastname: Damotharan
authors.forename: Anguchamy
authors.initials: A
authors.lastname: Veeruraj
authors.forename: Muthuvel
authors.initials: M
authors.lastname: Arumugam
authors.forename: Thangavel
authors.initials: T
authors.lastname: Balasubramanian
mesh_terms: D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D004546:Elapid Venoms / Q000201:enzymology*; D017815:Elapidae; D053878:Hemolytic Agents / Q000302:isolation & purification*; D010447:Peptide Hydrolases / Q000302:isolation & purification*
chemical_list: D004546:Elapid Venoms; D053878:Hemolytic Agents; D010447:Peptide Hydrolases
keywords: Cytotoxicity; Enhydrina schistosa; Hemolytic activity; Proteolytic activity; Sea snakes venom