Amrita Research Institute

Cochin, India

Amrita Research Institute

Cochin, India

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Saravanan R.,University of Madras | Santhi K.,University of Madras | Sivakumar N.,Amrita Research Institute | Narayanan V.,University of Madras | Stephen A.,University of Madras
Materials Characterization | Year: 2012

Zinc oxide nanorods and diluted magnetic semiconducting Ni doped ZnO nanorods were prepared by thermal decomposition method. This method is simple and cost effective. The decomposition temperature of acetate and formation of oxide were determined by TGA before the actual synthesis process. The X-ray diffraction result indicates the single phase hexagonal structure of zinc oxide. The transmission electron microscopy and scanning electron microscopy images show rod like structure of ZnO and Ni doped ZnO samples with the diameter ~ 35 nm and the length in few micrometers. The surface analysis was performed using X-ray photoelectron spectroscopic studies. The Ni doped ZnO exhibits room temperature ferromagnetism. This diluted magnetic semiconducting Ni doped ZnO nanorods finds its application in spintronics. © 2012 Elsevier Inc. All rights reserved.


Xavier T.,Amrita Research Institute | Sreepriya,Amrita Research Institute | Ganesan T.S.,Amrita Research Institute | Menon K.N.,Amrita Research Institute
Electrophoresis | Year: 2010

Sample preparation is one of the major issues in 2-DE for the separation of proteins. Although a 100% representation of cellular proteins onto a 2-DE is virtually impossible, maximum representation of cellular proteins compared with the original cell lysate is important in the subsequent analysis. We demonstrate that lysis of cells in urea/thiourea solution with subsequent sonication to disrupt the nucleic acids and concentration of the lysate using centri-con led to enrichment of proteins. The procedure resulted in minimal nucleic acid contamination with better resolution of spots. 2-DE spot patterns of proteins prepared using urea - thiourea solubilization/centri-con method to other protein enrichment methods such as phenol/chloroform/isoamyl alcohol extraction, methanol/ammonium acetate precipitation, acetone precipitation and ethanol precipitation were compared. Urea - thiourea solubilization combined with centri-con method of protein enrichment represented higher number/unique spots particularly in the 50-250 kDa Mr compared with others. Lysis of cells in urea/thiourea from the beginning of lysate preparation preserves the proteins from protease activity due to denaturation of proteases. Thus, we demonstrate that the centri-con methodology is simple and effective for the preparation of high-quality sample that can be used for a qualitative representation of cellular proteins on a 2-DE for proteomic analysis. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.

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