420 Matching Annotations
- Jul 2019
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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MP14:
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Germination of N.sativaseeds
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Cytotoxicity assay by Sulphorhodamine B (SRB) me
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Germination of N. sativaseeds
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Activation of TLC plate
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Tests for Alkaloids
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Germination of N.sativaseeds
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Testing of bioformulations
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Sequence analysis
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DNA sequencing of the 18S rDNA fragment
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Purification of PCR product
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Analysis of internal transcribed spacer region
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RAPDand SSRscoring and data analysis
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PCR amplification
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Running of gel and visualization of DNA
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Determination of the yield
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Agarose gel electrophoresis
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Qualitative and quantitative estimation of DNA
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Determination of the yield
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Procedure for DNA isolation
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Reagents required for fungal DNA isolationand p
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DNA isolation of Trichodermaisolate
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Genetic variability analysis through RAPD and SSR
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Photography, evaluation and documentation
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Procedurefor SDS-PAGE
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Materialsrequired for SDS-PAGE
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Protein profiling of bioagent through SDS-PAGE
Tags
- md-1-md-2
- md-1-md-2-mt-2
- md-1-md-2-mt-3
- md-2
- md-12-md-2
- md-2-md-11-md-1-md-4
- md-2-md-11-md-1-md-3
- md-2-md-11-md-1-md-9
- md-2-md-11-md-1-md-10
- md-2-md-11-md-1-md-7
- md-2-md-11-md-1-md-12
- md-2-md-11-md-1-md-2
- md-2-md-11-md-1-md-1
- md-2-md-11-md-1-md-5
- md-2-md-11-md-1-md-8
- md-2-md-11-md-1-md-11
- md-2-md-11-md-1-md-6
- md-2-md-1
- md-1-md-2-mt-1
Annotators
URL
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sg.inflibnet.ac.in sg.inflibnet.ac.inChapter 337
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Active site prediction and docking study
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Superposition of predicted structure and template (Dof
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Validations
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Three dimensional structure prediction, refinements and evaluation of Dof proteins
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Cis-regulatory element analysis
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Mapping of SbDof genes on sorghum chromosomes and its intron/exon gene structure prediction
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In silico prediction of Dof gene family members in S. bicolor (L
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Motif identification
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Multiple sequence alignment and phylogenetic analysis
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In silico analysis of sequenced Dof domain and Dof genes
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Reaction resuspension
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Post-reaction clean up
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Sequencing PCR
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Sequencing reaction
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Digestion of Plasmid DNA
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Minipreparation of plasmid DNA from transformed co
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Screening of recombinant E. coli clone
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Transformation of ligation mixture in electro-competent E. coli host cells (DH5ααααstrain)
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Transformation of ligated product in chemically competent E. coli host cells (DH5αααα strain)
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Ligation reactions
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Dephosphorylation of vector
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Restriction digestion
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Ligation of eluted PCR product in pBSK vector
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Cloning of gel eluted PCR produc
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Gel elution of PCR Produ
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Scoring of amplification data points and construction of a den
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Analysis of PCR amplicons using agarose gel electrophoresis
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Cycling condition
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PCR reaction set up
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Basic requirements for PC
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PCR amplification of Dof domain and Dof genes from different
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Primer designing for PCR amplification of Dof domain and D
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Qualitative analysis of DNA by agarose gel electrophoresi
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Spectrophotometric quantification of genomic DNA
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DNA purification
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DNA extraction procedure
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Isolation of genomic DNA by CTAB method
Tags
- md-2-md-12
- md-2-md-7-md-2-md-1
- md-2-md-7-md-2-md-3
- md-2-md-6-md-1
- md-2-md-7-md-5-md-1
- md-2-md-6-md-5
- md-2-md-8-md-2
- md-2-md-13
- md-2-md-7-md-5
- md-2-md-6-md-2
- md-2
- md-2-md-12-md-2
- md-2-md-7
- md-2-md-9
- md-2-md-7-md-4
- md-2-md-6-md-3
- md-2-md-11
- md-2-md-3
- md-2-md-2
- md-2-md-8-md-3
- md-2-md-13-md-3
- md-2-md-6-md-4
- md-2-md-4
- md-2-md-10
- md-2-md-5
- md-2-md-13-md-2
- md-2-md-7-md-5-md-2
- md-2-md-13-md-1
- md-2-md-6-md-6
- md-2-md-7-md-2
- md-2-md-12-md-1
- md-2-md-8
- md-2-md-7-md-3
- md-2-md-7-md-2-md-2
- md-2-md-1
- md-2-md-6
- md-2-md-8-md-1
Annotators
URL
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Nitrite production in macrophages of hamsters
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Animals
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Overexpression and Purification of recombinant protein (rLdTP
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Clone confirmation
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Colony PCR
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Transformation
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Assay for Lipid peroxidase(LPO)
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Cytomorphological analysis
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Growth kinetic studies
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Reducing power assay
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TEM-EDAX analysis
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Qualitative analysis of compounds
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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The Posterior Probability of Mixing Dis-tribution
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Algorithm
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EM Procedure
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Poisson Mixture
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Data Sources
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Poisson Model
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Haemolymph protein profiling
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Lactate dehydrogenase
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VS preparation
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Statistical analysi
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Quantification of VS for protein
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Venomous saliva utilization
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Prey type
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Starvation and collection method
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Venomous saliva optimization
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Insects Collection
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Head and stylet preparation
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Micronuclei test
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Malic dehydrogenase
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Alkaline Phosphatase
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Glycogen content
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Analysis of Physico-chemical parameters of the water sampled
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Experimental Set up
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- Jun 2019
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krishikosh.egranth.ac.in krishikosh.egranth.ac.in
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Soil pH and electrical conductivity (EC)
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Experiment 2: Assessing the impacts of elevated temperature and N levels on yield and nutrient uptake in rice
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Experiment 1: Assessing the impacts of elevated CO2and N levels on yield and nutrient uptake in rice
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Experimental Design and Treatments
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Temperature Gradient Tunnels (TGT)
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krishikosh.egranth.ac.in krishikosh.egranth.ac.in
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Kernel hardness
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SDS-sedimentation test
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Estimation of total N% of wheat grainsand straw
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End use Quality parameters
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Chlorophyllcontent
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Root length (cm) and Root weight (mg)
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Coleoptile length(cm)
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Stomata / cm2
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Leaf area index (LAI)
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Physiological parameters
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Laboratory observations
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Days to physiological maturity
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Static and shaken condition
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Screening for proteolytic activity
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Sample Collection
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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1X TBS
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Immunofluorescence
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Transfection of short interfering RNA (siRNA) and plasmid
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Mice
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.inThesis14
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Extraction of Tannin
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Extraction
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Procedure
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Standard curve of sugar
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Extraction and determination of protein
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Standard curve of protein
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Reagents
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Estimation of protein
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Standard curve of ascorbic acid
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Fresh and Dry weight
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Dilution Formula
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Cd (NO3)2
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ZnSO4
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Preparation of ppm solution
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Preparation of ultra competent E. coli
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Monoclonal Antibodies against the Human Glycophorin-
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Isolation of endothelial cells from rat aorta
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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Procedur
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Procedur
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Procedure
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Procedure
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Reagent
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Total antioxidant activit
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Procedur
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Catalyst Preparation
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Catalyst Preparation
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Total dissolved solids
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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High Performance Liquid Chromatography (HPLC) analysis
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High Performance Thin Layer Chromatography (HPTLC) analysis
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. Thin Layer Chromatography (TLC) analysis
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Preliminary phytochemical screening (Ali, 1998; Evans, 2002)
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Microbial Contamina
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Foaming Index
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pH values
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Ash values
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Extractive value
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. Physico-chemical standardization
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Standardization of ethanolic extract of E.ribes (WHO, 1998; IndianPharmacopoeia, 1996)
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Estimation of Stevioside
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Estimation of Steviol
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Estimation of total phenols
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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Balanced mesomorph:
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sg.inflibnet.ac.in sg.inflibnet.ac.in
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The [3-PMB and a-PMB chains were eluted with a linear gradient of 500 ml each of 0.01 M potassium phosphate buffer (pH 6.5) and 0.015 M potassium phosphate buffer (pH 8.5) at a flow rate of 50 ml/hour. The chains were separately concentrated using Centriprep concentrators (Amicon) and stored in liquid nitrogen till further use
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The heme bound a and ~ subunits were obtained as described by Bucci (1981 ). Briefly, hemoglobin was reacted with PMB in an eight fold molar excess (8 moles of PMB per mole of hemoglobin). The reaction mixture was dialyzed extensively against 0.01 M potassium phosphate buffer (pH 6.5) and then loaded onto a CM52 column (30cm x !Scm) that was pre-equilibrated with the same buffer.
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Separation of the a and f3 subunits of hemoglobin
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- May 2019
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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1X PBS diluted in distilled water 1X fixative solution diluted in distilled water 2.4.12.3 Staining Solution25 μl Solution A 25 μl Solution B 25 μl Solution C 125 μl 20 mg/ml X-gal in DMF
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Working Solutions:
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Procedure:
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β- galactosidase assay was performed in a 96 well format. Briefly, 4000-5000 cells were plated in 96 well tissue culture coated plate. Cells were transfected with reporter plasmid after 18 -24 hrs and after 48 hrs the cells were washed once with D-PBS. 50μl of lysis buffer was added to the well and cells were lysed by freezing plate at -70°C and thawing at 37°C. Cells were pipette up and down and then the plate was centrifuged at 9000 X g for 5 minutes. The supernatant from each plate was transferred to clean eppendorf tube. Immediately prior to assay the ONPG cocktail was prepared as below: 47 μl 0.1 M sodium phosphate (pH 7.5)22 μl 4 mg/ml ONPG1 μl 100X Mg solution30μl of each well extract was added to microtitre well plate and70μl of ONPG cocktail was added to each well. The plate was kept on ice throughout the procedure. After addition of ONPG cocktail the plate was transferred to 37°C and the development of colour was monitored every 10 minutes for development of color. After development of yellow colour, the reaction was stopped by addition of 150μl of 1M sodium carbonate to each well
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ethanol has dried. The pellet was resuspended in 20 μl of milliQ water and 20 μg/ml RNase added. The tube was incubated at 50°C for 45 min. the tube was vortexed for few seconds. Quality of the plasmid DNA was then accessed by running 1% agarose gel.
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Overnight Grown culture was pelleted by centrifugation at 10,000g at 4°C for 3 min and the supernatant was discarded. Pellet was resuspended in 250 μl of ice-cold alkaline lysis solution 1. 300 μl of alkaline solution 2 was then added and the tube was inverted gently 3-4 times and incubated at room temperature for 5 min. 350 μl of ice cold solution 3 was added and mixed by inverting the tube rapidly for 3 or 5 times. Suspension was incubated on ice for 10 min. Bacterial lysate was spun at 10,000g for 12 min at 4°C. Supernatant was transferred to a fresh tube. 0.4 volume of phenol: chloroform was added to the supernatant and the contents mixed. It was then spun at 10,000g at 4°C for 12 min. Aqueous phase was taken out in a fresh tube and 0.6 volume of isopropanol was added, mixed properly and incubated at room temperature for half an hour followed by spinning at 10,000g at RT for 20 min. Supernatant was discarded. Pellet was washed with 70% ethanol. The tube was stored at room temperature until the
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Preparation of Plasmid DNA by alkaline lysis
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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1μl of the cell lysate was mixed with 200 μl of 5X Bradford reagent and 800 μl of water. O.D was measured at 595 nm. Standard curve of BSA was plotted using various dilutions of BSA protein by Bradford method. Protein estimation of the cell lysate samples was performed using the standard curve equation y=0.0695x + 0.0329 μg/μl
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Protein estimation by Bradford method
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Overnight cell culture raised in LB medium was subcultured 1:100 in LB with 20 mM MgCl2. When the A600 reached 0.4-0.6, the culture was centrifuged at 2800g for 5 min at 4 ̊C. To the cell pellet 0.4 volumes of ice-cold TBF-I buffer was added and incubated on ice for 15 min. The cell suspension was centrifuged at 2800g for 5 min at 4 ̊C and the cells recovered were dissolved in 0.04 volume of ice-cold TBF-II buffer and kept on ice for 45 min. 100 μl aliquots of these competent cells were used for transformation using the normal transformation protocol
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TBF method for preparation of high competency cells
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Quiagen/HiPura following the manufacturer's protocols
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The rapid alkaline lysis method of plasmid isolation, as described by Sambrook and Russel (2001), was followed with minor modifications. Bacterial pellet from 3 ml of stationary-phase culture was resuspended in 200 μl of ice-cold solution I (50 mM glucose, 25 mM Tris-Cl pH 8.0, 10 mM EDTA pH 8.0 containing 1 mg/ml lysozyme) by vortexing. After 5 min incubation at room temperature, 400 μl of freshly prepared solution II (0.2 N NaOH, 1% SDS) was added and the contents were mixed, by gently inverting the tube several times. This was followed by the addition of 300 μl of ice-cold solution III (5 M potassium acetate, pH 4.8) and gentle mixing. The tube was incubated on ice for 5 min and centrifuged at 20,0000g for 15 min at 4°C. The clear supernatant was removed into a fresh tube and, if required, was extracted with an equal volume of phenol:chloroform mixture. The supernatant was precipitated with either two volumes of cold 95% ethanol or 0.6 volumes of isopropanol at room temperature for 30 min. The nucleic acids were pelleted by centrifugation, washed with 70% ethanol, vacuum dried, and dissolved in appropriate volume of TE buffer. If required, the sample was treated for 30 min with DNase free RNase at a final concentration of 20 μg/ml. The plasmid DNA was checked on a 0.8% agarose gel and stored at −20°. The plasmid DNA thus isolated was suitable for procedures such as restriction digestion, ligation, and preparation of radiolabeled probes. Plasmid isolation was also done with any of the commercially available kits from
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Isolation of plasmid DNA
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dependent transcription termination within the untranslated region of trpE. Anthranilate is a precursor of tryptophan, which is the product of trpE-encoded anthranilate synthase. Therefore, in trpE(fs) strains, growth on minimal glucose plates supplemented with anthranilate (100 μg/ml) reflects transcriptional polarity relief at the trp locus, and the same was scored after streaking the relevant strains on such medium
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The trpE9777 is a frameshift (fs) mutationconfers Trp auxotrophy and also polarity on the downstream trpDCBA genes in the operon due to premature Rho-
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trpE(fs) assay
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This test was therefore used for two purposes: (i) to distinguish relA+ from relA− strains, and (ii) as a qualitative measure of transcriptional polarity relief at the ilv locus. Growth in the presence of amino acids Serine, Methionine, and Glycine (SMG) was scored on glucose-minimal A plates supplemented with each of the amino acids at 100 μg/ml and compared with the growth on non-supplemented glucose-minimal A plates to score for SMG phenotype
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The E. coli relA mutants exhibit SMG-sensitive (SMGS) phenotype i.e. growth-inhibition in the presence of Serine, Methionine and Glycine at 1 mM concentration each (Uzan and Danchin, 1978) and is proposed to be a consequence of transcriptional polarity exerted by a frameshift mutation in the ilvG gene on the expression of downstream genes of the ilvGMEDA operon (Lopes et al., 1989). It was observed in another study that the rho and nusG mutants that are defective for transcription termination conferred SMG-resistant (SMGR) phenotype in a relA1 strain (Harinarayanan and Gowrishankar, 2003)
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SMG resistance
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shodhganga.inflibnet.ac.in shodhganga.inflibnet.ac.in
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and a colourless upper aqueous phase. The upper aqueous phase in which RNA existsexclusively, was transferred to a fresh microfuge tube and RNA was precipitated byadding 0.5 ml of isopropyl alcohol for each ml of Trizol used. Samples were incubatedat 15 to 30ºC for 10-min and centrifuged at 12000 rpm for 10-min at 4ºC. RNA formeda gel like precipitate at the bottom of the tube. Supernatant was removed and RNA waswashed with 75% ethanol (by adding 1 ml of ethanol per ml of Trizolemployed). RNAcould be stored after this step in –20 or –70ºC for more than a year. RNA pellet was airdried for 15-to 30-min following which it was dissolved in nuclease free water. Theconcentrations and purity of RNA samples were determined spectroscopically as wellas by visual inspection on formaldehyde-agarose gel in MOPS buffer (Goodet al., 1996). Before loading onto the gel, RNA was mixed with loading buffer and heated at90ºC for 3-min
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For isolation of RNA, cells were grown in minimal A medium supplemented with 0.2%glucose upto A600of 0.6. Cells were harvested by centrifugation and total RNA wasisolated by using Trizol (Invitrogen) according to manufacturer’s instructions. 1 ml ofTrizol was used to lyse cells equivalent of approximately 4 ml of overnight culture.Homogeneous lysis was achieved by gentle pipetting repeatedly. The homogenized samples were incubated at room temperature for 5-min to permit complete dissociationof nucleoprotein particles. Following homogenization, 0.2 ml of chloroform for each 1ml Trizol reagent was added and vigorously shaken with hand for 15-sec and incubatedfurther for 3-min at RT. It was then centrifuged at 12000 rpm for 10-min at 4ºC, whichseparates out the homogenate into lower phenol chloroform phase (red), an interphase
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Isolation of total cellular RNA
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Protein concentrations were estimated by the method of Bradford (1976). The A595wasmeasured after complexation with Bradford reagent. Bovine serum albumin was usedas standard against whichthe unknown protein concentrations were estimated
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Protein estimation
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Typically 200-300 ng of DNA was used in each ligation reaction. The ratio of vector toinsert was maintained between 1:3 to 1:5 for cohesive end ligation and 1:1 for blunt endligation. The reaction was generally performed in 10 μl volume containing ligationbuffer (provided by the manufacturer) and 0.05 Weiss unit of T4-DNA ligase, at 16ºCfor 14-to 16-hrs. On using the rapid ligation kitfrom Fermentas, incubation was at 22ºC for 1-2 hrs
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Ligation of DNA
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PCR products were purified using the PCR Purification Kit (Qiagen) as per the manufacturer's instructions
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DNA fragments to be used for specific purposes like ligation or radioactive labeling were eluted from the agarose gel after electrophoresis. The gel piece containing thedesired band was sliced out from the gel and the DNA was purified using commerciallyavailable purification kits for this purpose. The efficiency of elution was determined bychecking a small aliquot of DNA sample on the gel
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Purification of PCR products
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Purification of DNA by gel elution
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Around 0.5 to 1 μg of DNA was regularly used for each restriction digestion. 2to 5units of restriction enzyme were used in the total reaction volume of 20 μl containing 2μl of the corresponding buffer supplied at 10 X concentration by the manufacturer. Thereaction was incubated for 2 hrs at the temperature recommended by the manufacturer.The DNA fragments were visualised by ethidium bromide staining after electrophoresison a 0.8 to 1% agarose gels. Commercially available DNA size markers were run alongwith the digestion samples to compare with and to estimate the sizes of the restrictionfragments
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