Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Department of Social Sciences

Forty seven positive clinical mastitis milk samples of Streptococcus spp. were obtained from cows in and around Ranchi. They were treated in vitro with levofloxacin, ceftriaxone, amikacin and ampicillin and thereafter a smear was prepared, dried and subjected to acridine orange staining. Quantitative analysis of the effects of different antibacterial agents on bacterial phagocytosis and intracellular killing and degradation was done by acridine orange fluorescence technique. The present study revealed that ceftriaxone and amikacin proved to be better for parentral application due to their higher bactericidal and poor leucocidal property. Levofloxacin is a better choice for intra mammary use because of its better leucocidal and bactericidal property.

World University root node

School of Social Sciences & Languages

Vellore Campus

Indian Veterinary Journal

Use of acridine orange phagocytic function test in streptococcus spp. infected mastitic milk in selection of antibiotics

Chemotherapeutic management of extragenital transmissible venereal tumor in a dog

The agricultural sector of India, which witnessed a spectacular achievement in the production of foodgrains and other commodities over the last fifty years, is at the crossroads today. The crop holiday, which is never heard in the history of Indian agriculture, declared by the farmers neither belongs to rainfed areas nor the drought-prone regions but are from the districts of highly irrigated regions in Andhra Pradesh. The farmers leading the crop holiday campaign have also urged their peers in Punjab, Tamil Nadu and Karnataka to go on crop holiday so as to protest against the poor remuneration from paddy cultivation. Crop holiday is an issue which emerged only very recently in Indian agriculture. There could be many other new issues besides crop holiday that can also hamper the foodgrains production. Changes in land use pattern, irrigated area and area allotted for different foodgrain crop are important factors expected to affect the production of foodgrains.

Indian Journal of Agricultural Economics

India's new food security worries: From crop holiday to declining foodgrains area

Indian journal of gerontology

Inequality to elderly in social support at familial level: A socio-economic perspective

Aging brings about a number of physiological changes. It not only affects a person " s looks, but also becomes a cause of physical deterioration. This study was undertaken to understand the health status of elderly people and to gather some information about their perceived health needs using the information and over of Puducherry district. The present study is descriptive in nature. Herein, an attempt is made to describe the situation and major health problems faced by the elderly from 213 elderly population of aged 60 and above in three rural communes of Puducherry. Findings reveal that majority of the elderly, both male and female, are unhealthy. The most common health problems aged people face include eye sight, hearing, joint pains, nervous disorders, weakness, heart complaints, asthma, tuberculosis, skin diseases, urinary problems and others. More health problems were reported by women compared to men.

International Journal of Research in Social Sciences

Health problems of aged people

VIT Unitversity

Indian Journal of Applied Research

An Analytic study of Inflation in India

The intracellular enzyme dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52) from Pseudomonas aeruginosa is a potential drug target because it is essential for the growth of bacteria while it is absent in humans. Therefore, in order to design new compounds using structure based approach for inhibiting the function of DHDPS from P. aeruginosa (Ps), we have cloned, characterized biochemically and biophysically and have determined its three-dimensional structure. The gene encoding DHDPS (dapA) was cloned in a vector pET-28c(+) and the recombinant protein was overexpressed in the Escherichia coli host. The Km values of the recombinant enzyme estimated for the substrates, pyruvate and (S)-aspartate-β-semialdehyde [(S)-ASA] were found to be 0.90±0.13mM and 0.17±0.02mM, respectively. The circular dichroism studies showed that the enzyme adopts a characteristic β/α conformation which is retained up to 65°C. The fluorescence data indicated the presence of exposed tryptophan residues in the enzyme. The three-dimensional structure determination showed that DHDPS forms a homodimer which is stabilized by several hydrogen bonds and van der Waals forces at the interface. The active site formed with residues Thr44, Tyr107 and Tyr133 is found to be stereochemically suitable for catalytic function. It may be noted that Tyr107 of the catalytic triad belongs to the partner molecule in the dimer. The structure of the complex of PsDHDPS with (S)-lysine determined at 2.65Å resolution revealed the positions of three lysine molecules bound to the protein. © 2011 Elsevier B.V.

Centre for Bio-Separation and Technology

International Journal of Biological Macromolecules

Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa

Crystal of Russell Viper venom phospholipase A2 complexed with an isoquinoline alkaloid, berberine from a herbaceous plant Cardiospermum halicacabum, was prepared and its structure was solved by X-ray crystallography. The crystal diffracted up to 1.93 Å and the structure solution clearly located the position of berberine in the active site of the enzyme. Two hydrogen bonds, one direct and the other water mediated, were formed between berberine and the enzyme. Gly 30 and His 48 made these two hydrogen bonds. Additionally, the hydrophobic surface of berberine made a number of hydrophobic contacts with side chains of neighboring amino acids. Surface Plasmon Resonance studies revealed strong binding affinity between berberine and phospholipase A 2. Enzyme inhibition studies proved that berberine is a competitive inhibitor of phospholipase A2. It was inferred that the isoquinoline alkaloid, berberine, is a potent natural inhibitor of phospholipaseA 2. © 2011 Elsevier B.V. All Rights Reserved.

Biochimica et Biophysica Acta - Proteins and Proteomics

Identification of a novel and potent inhibitor of phospholipase A 2 in a medicinal plant: Crystal structure at 1.93 Å and Surface Plasmon Resonance analysis of phospholipase A2 complexed with berberine

Snake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l-amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A 2. Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure-based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non-enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitor-enzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications. Snake venoms are cocktails of enzymes and non-enzymatic proteins. Here, we describe the structures of the common snake venom enzymes, namely, acetylcholinesterase, L-amino acid oxidase, phospholipase A2, serine proteinase, and metalloproteinase, and their complexes. We discuss the contribution of these structures in understanding the mechanisms of catalysis and inhibition as well as in the structure-based design of new, potent inhibitors © 2011 The Authors Journal compilation © 2011 FEBS.