Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

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• 作者：Palani Damotharan ; Anguchamy Veeruraj…
• 关键词：Venom ; Hemolytic ; Proteolytic activity ; Activated partial thromboplastin time (APTT) ; Thrombin time (TT) ; Prothrombin time (PT)
• 刊名：Indian Journal of Clinical Biochemistry
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：31
• 期：1
• 页码：57-67
• 全文大小：781 KB
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• 作者单位：Palani Damotharan (1) (3)
  Anguchamy Veeruraj (1) (2)
  Muthuvel Arumugam (1)
  Thangavel Balasubramanian (1)
  
  1. Faculty of Marine Sciences, Centre of Advanced Study in Marine Biology, Annamalai University, Parangipettai, 608 502, India
  3. Marine Biotechnology, National Institute of Ocean Technology (NIOT), Ministry of Marine Science Govt. of India, Chennai, 600 100, India
  2. Centre for Ocean Research, (SU-NIOT Joint Initiative Research Centre), Sathyabama University, Rajiv Gandhi Salai, Chennai, 600 119, India
  
• 刊物主题：Biochemistry, general; Microbiology; Chemistry/Food Science, general; Pathology;
• 出版者：Springer India
• ISSN：0974-0422

文摘

This study is designed to isolate and purify a novel anti-clotting protein component from the venom of Enhydrina schistosa, and explore its biochemical and biological activities. The active protein was purified from the venom of E. schistosa by ion-exchange chromatography using DEAE-cellulose. The venom protein was tested by various parameters such as, proteolytic, haemolytic, phospholipase and anti-coagulant activities. 80 % purity was obtained in the final stage of purification and the purity level of venom was revealed as a single protein band of about 44 kDa in SDS-polyacrylamide electrophoresis under reducing conditions. The results showed that the Potent hemolytic activity was observed against cow, goat, chicken and human (A, B and O positive) erythrocytes. Furthermore, the clotting assays showed that the venom of E. schistosa significantly prolonged in activated partial thromboplastin time, thrombin time, and prothrombin time. Venomous enzymes which hydrolyzed casein and gelatin substrate were found in this venom protein. Gelatinolytic activity was optimal at pH 5–9 and 1H NMR analysis of purified venom was the base line information for the structural determination. These results suggested that the E. schistosa venom holds good promise for the development of novel lead compounds for pharmacological applications in near future. Keywords Venom Hemolytic Proteolytic activity Activated partial thromboplastin time (APTT) Thrombin time (TT) Prothrombin time (PT)