WIRELESS DIGITAL ELECTRONIC NOTICE BOARD USING WI-FI

The main objective of this project is to develop a notice board system using an Arduino board with Wi-Fibeing remotely controlled by any Android OS smart phone. As technology is advancing so information isalso getting smarter and scrolling. Modern information isgradually shifting from conventional notice board to centralized control system, involving Wi-Fi system. Presently, conventional notice board located in different location makes it difficult for the user to go near them to operate. In this system we are using Arduino master as main controller and remaining four Arduino as slave. When information is given through Wi-Fimaster arduino takes receives data from wi-fi according to coding it feds to slave arduino and display on LED notice board at same time information gradually shifting with controlled by shift register. With help of shift register data moving from one location to next location like this gradually scrolling. In system all slave lines are displaying different data with scrolling received from master

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Not AvailableA primary epicardial haemangiosarcoma (HSA) was identified in a 5-year-old female camel. Grossly the epicardium was completely covered by a thin fatty layer, over which multiple, cauliflower like, unencapsulated, soft, friable, haemorrhagic tumour outgrowths were attached. The pericardial cavity contained large amount of haemorrhagic effusion along with some fragments of neoplastic tissue. The impression smear of neoplastic tissue revealed pleomorphic, elongated, oval to spindle shaped tumour cells with hyperchromatic nuclei and moderately basophilic cytoplasm with vacuolations. The cytology smear from pericardial effusion revealed presence of large number of hypersegmented neutrophils (75%), few scattered neoplastic cells (20%) and lymphocytes (5%). The histopathology of tumour showed rich vascular tissue with unencapsulated and infiltrative tumour growth and haemorrhages. The argyrophilic nucleolar organizer region (AgNOR) count was found significantly more (P< 0.01) in cytology smear than histology section prepared from tumour tissue.Not Availabl

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Not AvailableBacterial esterases are gaining the importance in pharmaceuticals and agrochemical industries due to their excellent biocatalytic properties and a wide range of applications. In the present study, a novel gene encoding an esterase (designated as Est-CR) was identified from shotgun metagenomic sequencing data of camel rumen (Camelus dromedarius) liquor. The open reading frame consisted of 1,224bp, which showed 84.03% sequence identity to Bacteroidales bacterium, corresponding to a protein of 407 amino acids and has a catalytic domain belonging to an esterase. Est-CR belonged to family V with GLSMG domain. The purified enzyme with a molecular mass of 62.64 kDa was checked on SDS-PAGE, and its expression was confirmed by western blotting. The enzyme was active and stable over a broad range of temperature (35–65 °C), displayed the maximum activity at 50 °C and pH 7.0. Individually all metal ions inhibited the enzyme activity, while in combination, K2+, Ca2+, Mg2+ and Mn2+ metal ions enhanced the enzyme activity. The detergents strongly inhibited the activity, while EDTA (10 mM) increased the activity of the Est-CR enzyme. The enzyme showed specificity to short-chain substrates and displayed an optimum activity against butyrate ester. This novel enzyme might serve as a promising candidate to meet some harsh industrial processes enzymatic needs.Not Availabl

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Not AvailableBacterial esterases are gaining the importance in pharmaceuticals and agrochemical industries due to their excellent biocatalytic properties and a wide range of applications. In the present study, a novel gene encoding an esterase (designated as Est-CR) was identified from shotgun metagenomic sequencing data of camel rumen (Camelus dromedarius) liquor. The open reading frame consisted of 1,224bp, which showed 84.03% sequence identity to Bacteroidales bacterium, corresponding to a protein of 407 amino acids and has a catalytic domain belonging to an esterase. Est-CR belonged to family V with GLSMG domain. The purified enzyme with a molecular mass of 62.64 kDa was checked on SDS-PAGE, and its expression was confirmed by western blotting. The enzyme was active and stable over a broad range of temperature (35–65 °C), displayed the maximum activity at 50 °C and pH 7.0. Individually all metal ions inhibited the enzyme activity, while in combination, K2+, Ca2+, Mg2+ and Mn2+ metal ions enhanced the enzyme activity. The detergents strongly inhibited the activity, while EDTA (10 mM) increased the activity of the Est-CR enzyme. The enzyme showed specificity to short-chain substrates and displayed an optimum activity against butyrate ester. This novel enzyme might serve as a promising candidate to meet some harsh industrial processes enzymatic needs.Not Availabl