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325 results for “PURIFICATION”
Figure 3 in Purification Of Adult Hymenolepis Diminuta (Cestoda) Mitochondrial Nadph Nad Transhydrogenase
Figure 3. Effects of non-immune and immune IgG on the activity of membrane-associated and purified Hymenolepis diminuta transhydrogenase. Preparations and treatments are indicated as follows: Broken line and closed circles, mitochondrial membranes plus non-immune IgG; solid line and open circles, purified enzyme plus non-immune IgG; broken line and closed squares, mitochondrial membranes plus immune IgG; and solid line open squares, plus immune IgG. The activity of untreated mitochondrial membranes and purified enzyme was 0.12 and 8.3 µmol/ min/mg, respectively. Incubations were performed as described in Materials and Methods.
Figure 1 in Purification Of Adult Hymenolepis Diminuta (Cestoda) Mitochondrial Nadph Nad Transhydrogenase
Figure 1. SDS-PAGE of the purification of Hymenolepis diminuta transhydrogenase. Lane designation and amount of protein used were as follows: lane A, mitochondrial membranes, 30 µg; lane B, NaCl-washed membranes, 30 µg; lane C, detergent extract, 25 µg; lane D, DEAE Sepharose I, 5 µg; lane E, DEAE Sepharose II, 5 µg; lane F, hydroxylapatite, 5 µg. Relative positions of protein markers are indicated at the left. Protein was visualized as described in Materials and Methods.
Figure 2 in Purification Of Adult Hymenolepis Diminuta (Cestoda) Mitochondrial Nadph Nad Transhydrogenase
Figure 2. Immunoblot of Hymenolepis diminuta transhydrogenase. Lane designation, amount of protein used, and treatment were as follows: lane A, mitochondrial membranes, 30 µg plus non-immune IgG; lane B, mitochondrial membranes, 30 µg plus immune IgG; lane C, purified enzyme, 5 µg plus non-immune protein, IgG; lane D, purified enzyme, 5 µg plus immune IgG. Relative positions of protein markers are indicated at the left. Immunoblots were performed as described in Materials and Methods.
Design Strategies for Oxy-Combustion Power Plant Captured CO2 Purification
<p>This submission contains Aspen Plus files for the design and systems performance analysis of oxy-combustion power plant captured CO2 purification using different techniques.</p> <p>This data is taken from https://psecommunity.org/LAPSE:2021.0570</p>
Dataset for the paper "Deblending and Purification of Hydrogen from Natural Gas Mixtures using the Electrochemical Hydrogen Pump", International Journal of Hydrogen Energy, doi.org/10.1016/j.ijhydene.2023.05.065
<p>The data in this spreadsheet was used to produce the figures in the paper</p> <p>Authors:C Jackson, GT Smith, ARJ Kucernak</p> <p>Title:Deblending and Purification of Hydrogen from Natural Gas Mixtures using the Electrochemical Hydrogen Pump</p> <p>Journal:International Journal of Hydrogen Energy</p> <p>DOI:https://doi.org/10.1016/j.ijhydene.2023.05.065</p> <p>Please cite the above reference if you wish to use this data</p> <p>DOI of data:10.5281/zenodo.7963348</p>
Fig. 1 in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 1. Multiple sequence alignment of the amino acid sequence of PP2 proteins from Cucurbitaceae species as well as from A. thaliana and A. graveolens. Sequences of A. graveolens (CBC70481.1), A. thaliana (CAB78986.1), Coccinia indica agglutinin CIA17 (P0DSP5.1), Cucumis sativus (KAE8649724.1), Cucumis melo (AAM74924.1), Luffa acutangula (C0HJV2.1), Cucurbita argyrosperma (CBC70491.1), Cucurbita arg. sororia (AAM82558.1), Cucurbita moschata (AAF74345.1), Cucurbita pepo (023518987.1), Cucurbita maxima (AAA33117.1), Cucurbita digitata (AAM82559.1) were taken from NCBI gene bank. Multiple sequence alignment was performed using Clustal Omega (https://www.ebi.ac.uk/Tools/msa/clustalo/). The highly conserved amino acids 100-Leu-Ile-Glu-Val-Ser-Trp-105 and 199-Trp- Lys-200, which are important for chitooligosaccharide binding are shown in boxes. The residue numbers correspond to the primary structure of PPL.
Fig. 6 in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 6. Interaction of chitohexaose with the carbohydrate binding cleft of PPL, showing the amino acid residues involved in carbohydrate binding. The binding site was divided into three subsites as indicated by arrows: subsite 1 (Leu-100, Glu-102), subsite 2 (Ile-101, Ser-104, Trp-105) and subsite 3 (Trp-199, Lys- 200). Only three GlcNAc residues from the non-reducing end of chitohexaose are seen to interact with the binding cleft. GlcNAc residues at the reducing end interact with another PPL monomer (shown in the circle at the top left corner). Reproduced from Bobbili et al. (2014). Copyright (2014) Elsevier.
Fig. 3. A LigPlot depicting the interactions between CIA17 in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 3. A LigPlot depicting the interactions between CIA17 and bound chitotetraose. Adapted from the Supporting Information of Bobbili et al. (2019). Copyright (2019) Elsevier.
Fig. 5. A in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 5. A Complex of chitohexaose with PPL dimer obtained from molecular docking studies and optimized by molecular dynamics simulations. Reproduced from (Narahari et al., 2011b). Copyright (2011) American Chemical Society.
Fig. 7 in Isolation, purification, and characterization of pectin methylesterase inhibitor and polygalacturonase inhibitor protein from Indian lemon (Citrus limon L.)
Fig. 7. (a) Lineweaver-Burk plots of the inhibition of lemon PME by purified PMEI at different substrate concentrations (b) Lineweaver-Burk plots of the inhibition of lemon PG by purified PGIP at different substrate concentrations.
Fig. 1 in Isolation, purification, and characterization of pectin methylesterase inhibitor and polygalacturonase inhibitor protein from Indian lemon (Citrus limon L.)
Fig. 1. Elution profile of (a) PMEI and (b) PGIP by DEAE Sepharose anion exchange resin using 1 M NaCl.
Fig. 5 in Isolation, purification, and characterization of pectin methylesterase inhibitor and polygalacturonase inhibitor protein from Indian lemon (Citrus limon L.)
Fig. 5. (a) Logarithmic plot of residual inhibitory activity of purified extract of PMEI (b) Logarithmic plot of residual inhibitory activity of purified extract of PGIP (c) Arrhenius plot of purified PMEI (d) Arrhenius plot of purified PGIP (e) Plot of log D against the absolute temperature of purified PMEI (f) Plot of log D against the absolute temperature of purified PGIP.
Fig. 4 in Isolation, purification, and characterization of pectin methylesterase inhibitor and polygalacturonase inhibitor protein from Indian lemon (Citrus limon L.)
Fig. 4. (a) Effect of pH on the inhibitory activity of purified PMEI (b) Effect of pH on the inhibitory activity of purified PGIP (c) Effect of pH on the stability of purified PMEI (d) Effect of pH on the stability of purified PGIP (e) Effect of temperature on the inhibitory activity of purified PMEI (f) Effect of temperature on the inhibitory activity of purified PGIP.
Fig. 3 in Isolation, purification, and characterization of pectin methylesterase inhibitor and polygalacturonase inhibitor protein from Indian lemon (Citrus limon L.)
Fig. 3. MALDI-TOF mass spectra of (a) purified PMEI and (b) purified PGIP (m/z is mass-to-charge ratio; a.i. is absolute intensity).
Purification of High Molecular Weight DNA for Long-Read Sequencing Using a High-Salt Gel Electroelution Trap
<p><strong>Figure 3. Yield and purity of HMW DNA obtained from difficult samples using the method proposed in this study</strong>.</p> <p>(A) The proposed method extracts more HMW DNA from a complex soil sample than a commercial column purification kit. Shown is a negative image of an ethidium bromide-stained agarose gel. Lane 1: 1/10 aliquot of ~90 ng of HMW DNA isolated using the E.Z.N.A. soil DNA extraction kit from a soil sample containing ~1,5 μg of total DNA (HMW DNA yield around 6%). Lane 2: ~100 ng of CTAB-extracted DNA from the same soil sample. ~10 μg of this crude DNA preparation was used as input for HMW DNA purification using the proposed method. Lane 3: 1/100 aliquot of ~3 μg of HMW DNA isolated using the proposed method from ~10 μg of the CTAB-extracted DNA (HMW DNA yield around 30%).</p> <p>(B) The proposed method yields high-purity HMW DNA from a complex plant sample, as determined by agarose gel electrophoresis. Lane 1: molecular weight marker (GeneRuler DNA ladder, Thermo Fisher Scientific). Lane 2: crude nucleic acid preparation extracted with SDS/Proteinase K from <em>Zingeria trichopoda</em> leaves, which served as an input for HMW DNA purification using the proposed method. Lane 3: purified HMW DNA. Note the absence of low-molecular-weight nucleic acids and heavy covalent complexes in the purified sample.</p> <p>(C) Same as (B) except that crude, CTAB-extracted DNA from a complex soil sample was used as an input for HMW DNA purification. Note the absence of a continuous smear of fragmented DNA as well as heavy covalent complexes in the purified sample (lane 3). Molecular weight marker sizes are indicated in base pairs to the left of each panel.</p>
Home Air Purification for Eosinophilic COPD
ClinicalTrials.gov study NCT04252235. IPD Sharing: YES. Countries: 1. Publications: 1.
Effects of 21-day Purification Program on Healthy Adults
ClinicalTrials.gov study NCT05877365. IPD Sharing: Not stated. Countries: 1. Publications: 14.
Extracorporeal Blood Purification Therapy in Critically Ill Patients (GlobalARRT)
ClinicalTrials.gov study NCT04580680. IPD Sharing: NO. Countries: 1. Publications: 6.
Adaptive Blood Purification for the Treatment of Patients With Septic Shock
ClinicalTrials.gov study NCT06692036. IPD Sharing: YES. Countries: 1. Publications: 1.
Extracorporeal Blood Purification as a Treatment Modality for COVID-19
ClinicalTrials.gov study NCT04478539. IPD Sharing: NO. Countries: 1. Publications: 5.
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