The concentration of calcium ions at a solution pH of 1.5SBF (pH 7.4) was increased by 0.1, i.e., from pH value of 7.4 to 8.4, by adding Tris, which was measured by ICP-AES (ICPE-9000; Shimadzu, Tokyo, Japan). Moreover, the concentrations of calcium ions in the 1.5SBF at pH of 7.4, 7.7, 8.0, and 8.4 during incubation at 37 °C were also measured with the ICP-AES. Each solution with a different pH and incubation time was poured into a centrifuge tube and then centrifuged at 4640× g for 5 min. After the dispersed precipitates in the supernatant were removed by filtration through a microfilter (pore size, 0.22 μm, Millipore), the clear filtrate was collected in a tube and diluted in ultrapure water. Once 10-fold diluted solutions were preserved at 4 °C before measurement, 500-fold diluted solutions were measured by ICP-AES.
Microfilter
Manufactured by Merck Group
The Microfilter is a lab equipment designed to separate particles, cells, or other suspended solids from a liquid or gas. It utilizes a porous membrane to filter out the desired components while allowing the liquid or gas to pass through. The Microfilter's core function is to provide efficient and controlled filtration for various laboratory applications.
Automatically generated - may contain errors
Lab products found in correlation
Acquity uplc tqd system, by Waters Corporation (2 mentions)
Icpe 9000, by Shimadzu (1 mentions)
T 80 spectrophotometer, by PG Instruments (1 mentions)
C18 column, by Merck Group (1 mentions)
Labview, by National Instruments (1 mentions)
Beh amide column, by Waters Corporation (1 mentions)
Magna lyser, by Roche (1 mentions)
10 protocols using microfilter
1
Calcium Ion Concentration Measurement in Simulated Body Fluid
2
Extraction and Quantification of Amino Acids
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For the extraction of amino acids, 100 mg of shoot and root samples were homogenized in 80% aqueous ethanol for 1 min at 7000 g, spiked with norvaline, and centrifuged at 14,000× g for 20 min. The clear supernatant was vacuum-evaporated, and then the particle was resuspended in chloroform. The residual was then again extracted using HPLC-grade deionized water, centrifuged one more time, and the supernatant was mixed with the pellet suspended in chloroform. The centrifuged aqueous phase was filtered using a Millipore microfilter with a pore size of 0.2 M. (14,000× g, 10 min). We quantified amino acids using a Waters Acquity UPLC-tqd system (Milford) and a BEH amide column [31 (link)].
3
Mevastatin Extraction from Fermented Broth
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After fermentation, the harvested samples were homogenized to recover the product from broth. An equal volume of ethanol was added to fermentation broth and the suspension was kept in an incubated rotary shaker for 1 h at 200 rpm and 40 °C. The suspension was filtered through a Whatman filter paper and then through a micro filter (Millipore) of 0.22 mm pore diameter. 20 μL of the filtrate was analyzed for mevastatin using HPLC.
4
Quantitative Analysis of IL-6 and IL-6R
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Levels of human IL‐6 and IL‐6R in conditioned media of cultured cells were quantitatively determined in duplicate using an ELISA kit in accordance with the protocol from the manufacturer (both R&D Systems). Culture supernatants were collected and filtered through a micro‐filter (pore size, 0.22 μm; Millipore).
5
Evaluating Encapsulation Efficiency of Nano-Emulsions and Nano-Lipid Carriers
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To evaluate the encapsulation efficiency (EE) of the NE and the NLCs, an ultraviolet–visible spectroscopy method was used (Pivetta et al., 2018 (link)). For this aim, all samples were analyzed at the wavelength of maximum absorption of thymol in a T80+ spectrophotometer (PG Instruments, LTD., UK). Thereafter, the free thymol in the dispersion was quantified after centrifugation of the NE or the NLC dispersion using a microfilter (10,000 g/mol cutoff size, Millipore). The filtrate was diluted in ethyl alcohol (1:1) and then analyzed at a wavelength of 276 nm using the method previously described. The amount of thymol was calculated according to the following equation:
6
Quantification of Surfactin by HPLC
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After the culture samples were taken by centrifuge at 12,000× g for 15 min to remove the biomass, the concentration of surfactin in the supernatant was analyzed by reverse phase C18 HPLC at 30 °C, which is equipped with a Merck C18 column (5 μm) [18 (link)]. Prior to analysis, the samples were filtered through a Millipore microfilter (0.45 μm). A mixture of acetonitrile and 3.8 mM of trifluoroacetic acid (20 vol%) was used as the mobile phase, flowing at 1.0 mL/min. The sample (20 μL) was injected and analyzed at a wavelength of 205 nm using a UV detector (Jasco 975, Tokyo, Japan). Each analysis was duplicated under identical conditions, and the reproducibility was mostly within 5%.
Surfactin powder (98% purity as per label claim) directly obtained from Sigma Co. (St. Louis, MO, USA) was treated as the standard. The purity of surfactin in the sample taken in this study was determined by
Surfactin powder (98% purity as per label claim) directly obtained from Sigma Co. (St. Louis, MO, USA) was treated as the standard. The purity of surfactin in the sample taken in this study was determined by
7
Perfusion Bioreactor System Design
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The perfusion bioreactor system consisted of 2 chambers with a height of 50 mm and inner diameter of 20 mm (Figure 1). A frame with 15-mm-long, 6.3-mm-diameter crossbars on each end that were 45 mm apart and offset by 90° fit securely within each bioreactor chamber. Each chamber had a removable cap with a centrally located port (inner diameter, 3 mm) at the highest end. There was an identical port in the center of the lowest end of the chamber base. The lowest port of each bioreactor was attached to a port of a 10-mL medium reservoir (Synthecon) with tubing (Tygon; Saint-Gobain Performance Plastics; inner diameter, 4.8 mm) via a 3-way stopcock. The reservoir had an additional port (internal diameter, 3 mm) fitted with a microfilter (Millipore) for gas exchange. The port on each bioreactor cap was connected to a computer-controlled peristaltic pump (ISM404b; Ismatec) via 3-way stopcocks attached to 0.22-µm microfilters to which tubing (Tygon; Saint-Gobain Performance Plastics; inner diameter, 1.0 mm) between the bioreactor and pump was attached. System fluid flow rate and direction were controlled by a computer (LabView; National Instruments). All bioreactor system parts were sterilized with ethylene oxide prior to assembly and use.
8
Amino Acid Profiling of Plant Sprouts
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Amino acids were determined from 200 mg of sprouts combined with 1 mL of 80% (v/v) aqueous ethanol [24 (link)]. For accurate evaluation and correction of varied mass spectrometry reactions, norvaline was employed as an internal standard. The homogenate was centrifuged for 30 min at 14,000× g. The supernatant was added to fresh tubes and then dried. Next, chloroform (1 mL) was used for pellet resuspension followed by centrifugation (14,000× g for 30 min), then further extraction of the plant in water was performed and the extract was blended with the chloroform-suspended pellet. Then, the combined extract was centrifuged at 20,000× g for 10 min. Thereafter, the aqueous phase was filtered (Millipore microfilters, 0.2 μm pore size) for amino acid assessment. Amino acids were separated on a BEH amide 2.1 × 50 column (Waters Acquity UPLC-tqd system, Milford, MA, USA) [21 (link)]. A 10 μL sample was inserted and elution was carried out with a gradient of 0.1% formic acid (FA) in H2O and 0.1% formic acid in acetonitrile. The sample was kept at 20 °C and at a 30 °C column temperature.
9
Quantitative Amino Acid Analysis Protocol
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For amino acid analysis, the method described in [66 (link)] was used, in which 100 mg of each plant was homogenized in 5 mL of 80% ethanol at 5000 rpm for 1 min. After centrifugation (14,000× g for 25 min), the supernatant was resuspended in 5 mL of chloroform. Thereafter, 1 mL of H2O was used for the residue extraction. The supernatant and pellet were resuspended in chloroform and centrifuged at 8000× g for 10 min. A total of 15 amino acids (0.05 µmoles mL−1 for each one) were used as reference standards for determination of the retention time of each amino acid. An internal standard α-aminobutyric was also used for amino acid detection. Then, the extracts were centrifuged for 10 min at 20,000× g and the aqueous phase was filtered by Millipore micro-filters (0.2-lm pore size). The amino acids were quantified (using a Waters Acquity UPLC TQD device coupled to a BEH amide column, 2.1 mm × 50 mm). The elution (A, 84% ammonium formate, 6% formic acid, and 10% acetonitrile, v/v, and B, acetonitrile and 2% formic acid, v/v) resulted in amino acid peak integration. Star Chromatography (version 5.51) software was applied.
10
Plant Amino Acid Quantification by UPLC
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Amino acids were extracted by homogenizing plant shoots (200 mg FW) in 1 ml of 80% (v/v) aqueous ethanol (MagNALyser; Roche, Vilvoorde, Belgium; 1 min, 7000 rpm), spiked with norvaline to estimate the loss of amino acids during extraction, and centrifugation at 20 000 g for 20 min. The supernatant was vacuum‐evaporated, and the pellet resuspended in 1 ml of chloroform. The plant residue was re‐extracted with 1 ml HPLC grade water using MagNALyser and the supernatant after centrifugation (20 000 g for 20 min) was mixed with the pellet suspended in chloroform. Then the extracts were centrifuged for 10 min at 20 000 g and the aqueous phase was filtered by Millipore microfilters (0.2‐μm pore size) before assaying amino acid concentrations. Amino acids were measured by using a Waters Acquity UPLC‐tqd system (Milford, MA, USA) equipped with a BEH amide 2.1 × 50 column (Sinha et al., 2013 ).
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