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Your search keyword '"Gunwar, Sripad"' showing total 23 results
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23 results on '"Gunwar, Sripad"'

4. Circulating factor associated with increased glomerular permeability to albumin in recurrent focal segmental glomerulosclerosis

Author

Savin, Virginia J., Sharma, Ram, Sharma, Mukut, McCarthy, Ellen T., Swan, Suzanne K., Ellis, Eileen, Lovell, Helen, Warady, Bradley, Gunwar, Sripad, Chonko, Arnold M., Artero, Mary, and Vincenti, Flavio

Subjects
Glomerulonephritis -- Physiological aspects, Blood proteins -- Physiological aspects
Abstract

A chemical circulating in the plasma may be responsible for focal segmental glomerulosclerosis. Focal segmental glomerulosclerosis is a kidney disease characterized by scarring of the glomeruli, which are the part of the kidney that filters blood. Researchers took serum samples from 100 patients with focal segmental glomerulosclerosis and tested them in an assay using rat glomeruli. The permeability of rat glomeruli to the protein albumin was 0.18 when exposed to the patients' serum, compared to 0.06 when exposed to the serum of healthy volunteers. Some serum samples from patients with focal segmental glomerulosclerosis caused the permeability of rat glomeruli to jump to 0.50 or higher. Several patients were treated with plasmapheresis, a procedure in which plasma is replaced. Following plasmapheresis, their plasma lost the ability to increase the permeability of rat glomeruli. This indicates that a chemical in plasma may contribute to focal segmental glomerulosclerosis.

Published
1996

6. Immobilization of organophosphate hydrolase on biocompatible gelatin pads and its use in removal of organophosphate compounds and nerve agents

Author

Anantha KoteswaraRao, Kanugula, Elisha Raju, Repalle, Jay Prakash, Pandey, Gunwar, Sripad, Chanchal Kumar, Mitra, Devender Kumar, Dubey, and Dayananda, Siddavattam

Subjects
Insecticides, Organophosphorus Compounds, Hydrolysis, Enzyme Stability, Escherichia coli, Gelatin, Methyl Parathion, Enzymes, Immobilized, Sarin, Phosphoric Monoester Hydrolases, Substrate Specificity
Abstract

Bacterial organophosphate hydrolases (OPH) have been shown to hydrolyze structurally diverse group of organophosphate (OP) compounds and nerve agents. Due to broad substrate range and unusual catalytic properties, the OPH has successfully been used to develop eco-friendly strategies for detection and decontamination of OP compounds. However, their usage has failed to gain necessary acceptance, due to short half-life of the enzyme and loss of activity during process development. In the present study, we report a simple procedure for immobilization of OPH on biocompatible gelatin pads. The covalent coupling of OPH using glutaraldehyde spacer has been found to dramatically improve the enzyme stability. There is no apparent loss of OPH activity in OPH-gelatin pads stored at room temperature for more than six months. As revealed by a number of kinetic parameters, the catalytic properties of immobilized enzyme are found to be comparable to the free enzyme. Further, the OPH-gelatin pads effectively eliminate OP insecticide methyl parathion and nerve agent sarin.

Published
2011

10. Mutational analysis of single-stranded DNA templates active in the in vitro initiation assay for adenovirus DNA replication

Author

R. Padmanabhan, Gunwar Sripad, Larry Dobbs, and Ling-Jun Zhao

Subjects
DNA Replication, viruses, Molecular Sequence Data, Oligonucleotides, DNA, Single-Stranded, Biology, medicine.disease_cause, Oligomer, chemistry.chemical_compound, Virology, medicine, Humans, Binding site, Base Sequence, Point mutation, Adenoviruses, Human, DNA replication, Templates, Genetic, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, Molecular biology, Adenoviridae, Mastadenovirus, chemistry, Replication Initiation, DNA, Viral, Mutation, DNA, HeLa Cells, Plasmids
Abstract

Three distinct domains, A, the minimal origin, as well as B and C, the binding sites for the host nuclear factors, are required for efficient initiation of adenovirus (Ad) DNA replication at the termini. The initiation reaction was examined using partially purified nuclear extracts and various single-stranded oligomers as DNA templates. We observed that single-stranded oligomers containing Ad2 minimal origin (Ori) sequences (bp 1–18) from the I-strand of the Ad2 genome supported preterminal protein-dCMP complex formation in vitro. Using oligomers containing point mutations in the Ad2 minimal Ori sequence, six positions were identified as important to the function of the Ad2 minimal Ori sequence. Point mutations at position 7, 8, or 11 virtually abolished the ability of the oligomer to support the initiation reaction. Point mutations at position 4, 9, or 17 were found to decrease the ability of the oligomers to support the initiation reaction to 33, 67, and 58% of control, respectively. An oligomer complementary to the ]-strand of the Ad2 minimal Ori was found to block initiation on minimal ON template. A number of randomly selected nonspecific oligomers did not, in general, serve as templates for initiation with the exception of two oligomers, one of which was found to be about threefold more active than the control minimal Ori template. The biological significance of the in vitro initiation of Ad2 DNA replication on single-stranded DNA templates is discussed.

Published
1990

11. Type IV Collagen of the Glomerular Basement Membrane

Author

Boutaud, Ariel, primary, Borza, Dorin-Bogdan, additional, Bondar, Olga, additional, Gunwar, Sripad, additional, Netzer, Kai-Olaf, additional, Singh, Narinder, additional, Ninomiya, Yoshifumi, additional, Sado, Yoshikazu, additional, Noelken, Milton E., additional, and Hudson, Billy G., additional

Published
2000
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12. The Goodpasture Autoantigen

Author

Netzer, Kai-Olaf, primary, Leinonen, Anu, additional, Boutaud, Ariel, additional, Borza, Dorin-Bogdan, additional, Todd, Parvin, additional, Gunwar, Sripad, additional, Langeveld, Jan P.M., additional, and Hudson, Billy G., additional

Published
1999
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13. Glomerular Basement Membrane

Author

Gunwar, Sripad, primary, Ballester, Fernando, additional, Noelken, Milton E., additional, Sado, Yoshikazu, additional, Ninomiya, Yoshifumi, additional, and Hudson, Billy G., additional

Published
1998
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14. Seminiferous Tubule Basement Membrane

Author

Kahsai, Tesfamichael Z., primary, Enders, George C., additional, Gunwar, Sripad, additional, Brunmark, Charlott, additional, Wieslander, Jörgen, additional, Kalluri, Raghuram, additional, Zhou, Jing, additional, Noelken, Milton E., additional, and Hudson, Billy G., additional

Published
1997
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17. The pathogenesis of Alport syndrome involves type IV collagen molecules containing the α3(IV) chain: Evidence from anti-GBM nephritis after renal transplantation

Author

Hudson, Billy G., primary, Kalluri, Raghuram, additional, Gunwar, Sripad, additional, Weber, Manfred, additional, Ballester, Fernando, additional, Hudson, Julie K., additional, Noelken, Milton E., additional, Sarras, Michael, additional, Richardson, Walter R., additional, Saus, Juan, additional, Abrahamson, Dale R., additional, Glick, Alan D., additional, Haralson, Michael A., additional, Helderman, J. Harold, additional, Stone, William J., additional, and Jacobson, Harry R., additional

Published
1992
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23. Increased yield of high purity recombinant human interferon-gamma utilizing reversed phase column chromatography.

Author

Reddy PK, Reddy SG, Narala VR, Majee SS, Konda S, Gunwar S, and Reddy RC

Subjects
Chromatography methods, Chromatography, Gel, Cloning, Molecular, Culture Media, DNA Primers, Humans, Interferon-gamma blood, Interferon-gamma chemistry, Interferon-gamma genetics, Recombinant Proteins, Restriction Mapping, Solubility, Interferon-gamma isolation & purification
Abstract

Increasing therapeutic applications for recombinant human interferon-gamma (rhIFN-gamma), an antiviral proinflammatory cytokine, has broadened interest in optimizing methods for its production and purification. We describe a reversed phase chromatography (RPC) procedure using Source-30 matrix in the purification of rhIFN-gamma from Escherichia coli that results in a higher yield than previously reported. The purified rhIFN-gamma monomer from the RPC column is refolded in Tris buffer. Optimal refolding occurs at protein concentrations between 50 and 100 microg/ml. This method yields greater than 90% of the dimer form with a yield of 40 mg/g cell mass. Greater than 99% purity is achieved with further purification over a Superdex G-75 column to obtain specific activities of from 2 x 10(7) to 4 x 10(7)IU/mg protein as determined via cytopathic antiviral assay. The improved yield of rhIFN-gamma in a simple chromatographic purification procedure promises to enhance the development and therapeutic application of this biologically potent molecule.

Published
2007
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