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BACKGROUND Proteins with new function originate through gene duplication followed by divergence. In nature, occurrence of structurally and functionally similar proteins performing highly diverse physiological roles within an organism is rare. Several Australian elapid snakes have two parallel prothrombin activating systems with distinct physiological roles.(More)
BACKGROUND The evolution of structurally and functionally similar proteins with highly diverse physiological roles within a single organism is of great interest. Australian elapid snakes offer an excellent opportunity to study the molecular evolution of prothrombin activators. Venom from Pseudonaja textilis contains pseutarin C, a group C prothrombin(More)
Snake venom proteins belong to various families which differ in their primary and secondary structures. Recently , we found a novel transcript in the venom gland of Sistrurus catenatus edwardsii which was named " Ku-wap-fusin " because it encodes Kunitz-type serine protease inhibitors (Kunitz SPIs) and whey acidic protein (WAP) domains in tandem. We have(More)
Toxin profiling helps in cataloguing the toxin present in the venom as well as in searching for novel toxins. The former helps in understanding potential pharmacological profile of the venom and evolution of toxins, while the latter contributes to understanding of novel mechanisms of toxicity and provide new research tools or prototypes of therapeutic(More)
The origin and evolution of venom toxins is a mystery that has evoked much interest. We have recently shown that pseutarin C, a prothrombin activator from Pseudonaja textilis venom, is structurally and functionally similar to mammalian coagulation factor Xa-factor Va complex. Its catalytic subunit is homologous to factor Xa while the nonenzymatic subunit is(More)
Pea (Pisum sativum L.) lectin is known to have interesting pharmacological activities and of great interest on biomedical research. In the current research pea lectin was purified followed by ion exchange chromatography on DEAE column and affinity chromatography on glucose-sepharose column. The lectin shown 11.7-84% inhibitory effect against Ehrlich ascites(More)
The complete sequence characterization of snake venom proteins by mass spectrometry is rather challenging due to the presence of multiple isoforms from different protein families. In the present study, we investigated the tryptic digest of the venom of the viperid snake Sistrurus catenatus edwardsii by a combined approach of liquid chromatography coupled to(More)
The tuberous rhizome Kaempferia rotunda Linn. has been used as food and traditional medicinal plant, and the purified K. rotunda lectin (KRL) showed antiproliferative activity against Ehrlich ascites carcinoma cells [1]. In the present study, KRL showed agglutination activity against Escherichia coli and Staphylococcus aureus, with partial inhibition of(More)
UNLABELLED At present there is no well structured database available for the venomous snakes and venom composition of snakes in the world although venom has immense importance in biomedical research. Searching for a specific venom component from NCBI, PDB or public databases is troublesome, because they contain huge amount of data entries. Therefore, we(More)
In this study, the antioxidative fraction of white mulberry (Morus alba) was found to have an apotogenic effect on Ehrlich's ascites carcinoma cell-induced mice (EAC mice) that correlate with upregulated p53 and downregulated NFκB signaling. The antioxidant activities and polyphenolic contents of various mulberry fractions were evaluated by(More)