Total protein and amylose contents in matured grains were evaluated in each year from 2013 to 2018 using the methods of Hori et al. (2021b (link)). Apparent amylose content was determined using an Auto Analyzer II (Bran + Luebbe, Norderstedt, Germany). Crude protein content was determined by the combustion method with an induction furnace at 900 °C (American Association of Cereal Chemists International, Approved Method 46-30.01). Measurement of low-molecular-weight compounds was carried out in 2015 and 2016, using the methods of Human Metabolome Technologies (Tsuruoka, Japan). Briefly, rice flours from each line were homogenized in 600 µL methanol containing 10 µM internal standards, mixed with 600 µL chloroform and 240 µL water, then centrifuged at 2300 × g for 5 min. The aqueous supernatant fraction was filtered and recovered into 50 µL of MilliQ water prior to metabolite analysis using capillary electrophoresis time of flight-mass spectrometry (CE-TOFMS) (Agilent Technologies, CA, USA) (Soga et al. 2004 (link)). Peaks detected in the CE-TOFMS analysis were extracted using automatic integration software (MasterHands ver. 2.17.1.11) and annotated with putative metabolites based on their migration in CE and m/z values.
Milli q water
Manufactured by Agilent Technologies
Sourced in United States
Milli-Q water is a high-purity water system produced by Agilent Technologies. It uses a multi-stage purification process to remove impurities from water, resulting in ultrapure water with low levels of organic and inorganic contaminants. The core function of Milli-Q water is to provide consistently pure water for various laboratory applications.
Automatically generated - may contain errors
Lab products found in correlation
0.22 m spin filter tube, by Agilent Technologies (2 mentions)
Ce tofms, by Agilent Technologies (1 mentions)
Icp ms, by Agilent Technologies (1 mentions)
Nylon filter, by Agilent Technologies (1 mentions)
Hypersil aa ods column, by Agilent Technologies (1 mentions)
700 series icp oes, by Agilent Technologies (1 mentions)
6 protocols using milli q water
1
Quantifying Rice Grain Quality Traits
2
Dual Drug-Loaded Liposome Release Kinetics
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Dual drug‐loaded LbL NPs were incubated under sink conditions (1‐L sink for 1 mL of liposome suspension) in 1× PBS pH 7.4 or in citrate buffer pH 5.0 under agitation in 1 mL of 3500 MWCO Float‐A‐Lyzer (Spectrum) at 37°C. PBS or citrated buffer was replenished with the equivalent of sample taken each day of the experiment. Samples were taken of the liposomes to quantify remaining drug concentrations by for quantification. For quantification of cumulative release of AZD2281 and BMN 673 samples were vortex in 50:50 mixture of mobile phase of acetonitrile:water with 0.1% formic acid (pH 5). Samples were first separated by HPLC and analyzed by mass spectrometry. The separation was between absorbance of 180 and 240 nm for BMN 673 and 210 and 220 nm for AZD2281. For cumulative release cisplatin samples quantification, samples were diluted 200‐fold in MilliQ water and platinum content measured on ICP‐MS (Agilent Technologies). All samples were analyzed in triplicate.
3
Plasma Preparation for Proteomic Analysis
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Two microliters of raw plasma was diluted with 59 µl of Milli-Q water in a 0.22 µm spin filter tube (Agilent Technologies, USA) and spun at 14,000×g in a centrifuge (Micro 220R, Hettich, Germany) for 1 min. The diluted plasma samples were aliquoted into 10 µg samples and prepared for in-solution digestion.
4
Plasma Peptide Fractionation Protocol
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Two microliters of raw plasma was diluted with 59 µl of Milli-Q water in a 0.22 µm spin filter tube (Agilent Technologies, USA) and spun at 14,000×g in a centrifuge for 1 min. The diluted plasma was aliquoted into eight 10 µg samples and prepared for in-solution digestion.
After digestion, the peptides were fractionated using two different SCX systems, including a cartridge system (AB Sciex) and a spin system (Microspin; The Nest Group, Inc.), according to the manufacturer's instructions. The peptides were sequentially eluted from the columns with increasing KCl concentrations. Four fractions were collected in 100, 200, 350, and 500 mM KCl. Because the samples were fractionated into four fractions, the peptides from four pooled 10-µg samples were used for the SCX approach.
After digestion, the peptides were fractionated using two different SCX systems, including a cartridge system (AB Sciex) and a spin system (Microspin; The Nest Group, Inc.), according to the manufacturer's instructions. The peptides were sequentially eluted from the columns with increasing KCl concentrations. Four fractions were collected in 100, 200, 350, and 500 mM KCl. Because the samples were fractionated into four fractions, the peptides from four pooled 10-µg samples were used for the SCX approach.
5
Amino Acid Analysis for Enzyme Immobilization
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The analysis of amino acids was carried out to demonstrate enzyme immobilization. For that purpose, the immobilized enzyme was hydrolyzed with 6 M HCl using a Milestone ETHOS D microwave oven from Gomensoro (Madrid, Spain) under argon conditions at 170 °C for 20 min. After digestion, samples were diluted up to 10 mL with Milli-Q water and filtered with nylon filters (13 mm diameter and 0.45 μm pore size) from Agilent Technologies (Palo Alto, CA, USA). Amino acids were analyzed by RP-HPLC previous derivatization with OPA using a Hypersil AA-ODS column (2.1 mm × 200 mm, 5 μm particle size) from Agilent Technologies. OPA derivatization was carried out in the injector by mixing 8 μL of OPA, 6 μL of borate buffer, 4 μL of sample, and 6 μL of borate buffer. The reaction took 2 min and immediately after, samples were analyzed by RP-HPLC. The chromatographic conditions were: mobile phase A, sodium acetate (50 mM, pH 7.2); mobile phase B, ACN; injection volume, 24 μL; flow rate, 0.5 mL/min; column temperature, 20 °C; elution gradient, 0–50% B for 40 min, 50–90% B for 5 min, and 90% B for 5 min. Fluorescence detection was recorded at a λexc of 340 nm and a λem of 450 nm. Amino acid identification was carried out by comparison with amino acid standards.
6
Trace Metal Analysis in Fish Plasma
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The concentration of 13 metals was measured in the blood plasma from individual fish. The plasma samples were prepared to metal quantification according to the protocol developed by Goullé et al. (2005) . In the meantime, two tubes containing the international certified reference material (TORT-2 sample (Lobster hepatopancreas) and DOLT-4 samples (Fish liver)) were prepared in order to verify the accuracy of the method. Approximately 100 mg of those CRMs were digested by 3 mL of nitric acid in polypropylene tubes. Then, this mixture was heated by Hot Block for 3 hours at 100˚C, and after cooling 15 mL of ultrapure water (Milli-Q®) was added. Finally, 2 blank samples were also prepared in the same conditions (3 mL of HNO3 before heating and 15 mL of Milli-Q water added after cooling).
However, all metals were analysed by Inductively Coupled Plasma Optical Spectrometry (ICP-OES; Agilent Technologies, 700 Series ICP-OES).
However, all metals were analysed by Inductively Coupled Plasma Optical Spectrometry (ICP-OES; Agilent Technologies, 700 Series ICP-OES).
About PubCompare
Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.
We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.
However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.
Ready to get started?
Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required
Revolutionizing how scientists
search and build protocols!