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Sulfosalicylic acid

Sulfosalicylic acid is a chemical compound used in various research applications, including the analysis of proteins, detection of microalbuminuria, and as a precipitating agent.
It is a white crystalline solid with a melting point of approximately 202°C.
Sulfosalicylic acid is soluble in water and has a pKa value of 2.85, making it a useful reagent for acidic conditions.
Researchers can utilize PubCompare.ai's AI-driven platform to effeciently locate and compare published protocols for working with sulfosalicylic acid, identifying the best solutions to optimize their research workflows.

Most cited protocols related to «Sulfosalicylic acid»

1
Comprehensive Analysis of Ginseng Metabolites
Cited 13 times
Starch was measured via an enzyme hydrolysis method. Starch was hydrolyzed into dual sugars by amylase, hydrolyzed into monosaccharides by hydrochloric acid, and finally determined by reducing sugar, which is converted to starch (Rose et al., 1991 (link)).
The contents of pyruvate in the sample were determined according to the methods of Lin et al. (1995 ). Protein was removed from the samples by TCA precipitation, and in the resulting sample, pyruvate reacted with 2,4-nitrophenylhydrazine. The product turned red in the presence of an alkali solution, and the intensity of the color change was measured by a spectrophotometer. A standard curve for calibration was obtained using sodium pyruvate as a reagent with a gradient of concentrations of pyruvic acid. Absorbance values were obtained to generate a standard curve to calculate the pyruvate concentration.
For glutathione (GSH), roots were ground in liquid nitrogen and homogenized in 1 mL 5% (w/v) m-phosphoric acid containing 1 mM diethylene triamine pentaacetic acid (DTPA) and 6.7% (w/v) sulfosalicylic acid. Root extracts were centrifuged at 12,000 × g for 15 min at 4°C. GSH contents were determined according to the methods of Kortt and Liu (1973 (link)) and Ellman (1959 (link)) with some modifications.
The ascorbic acid (AsA) content was determined according to Egea et al. (2007 (link)) with slight modifications. Ginseng roots were ground in an ice bath with 10 mL 5% metaphosphoric acid stored at 4°C, and then the final mix was homogenized by vortex. The final solution was maintained on the ice bath, in darkness, for 30 min and then centrifuged at 20,000 × g for 25 min at 4°C. Ascorbate was spectrophotometrically detected by measuring absorbance at 254 nm with a UV detector. For quantification of the compound, a calibration curve in the range of 10–100 mg kg−1 was prepared from standard ascorbic acid. Results were expressed as mg 100 g−1 FW.
Root extracts were centrifuged at 12,000 × g for 15 min at 4°C. The extraction and determination of ginsenosides was performed following the method of Yu et al. (2002 (link)).
Ma R., Sun L., Chen X., Mei B., Chang G., Wang M, & Zhao D. (2016). Proteomic Analyses Provide Novel Insights into Plant Growth and Ginsenoside Biosynthesis in Forest Cultivated Panax ginseng (F. Ginseng). Frontiers in Plant Science, 7, 1.
Full text: Click here
Publication 2016
4-nitrophenylhydrazine Alkalies Amylase Ascorbic Acid Bath Carbohydrates Darkness Enzymes Ginseng Ginsenosides Hydrochloric acid Hydrolysis metaphosphoric acid Monosaccharides Nitrogen Pentetic Acid Phosphoric Acids Plant Roots Proteins Pyruvates Pyruvic Acid Sodium Starch Sugars sulfosalicylic acid
2
Comprehensive Oxidative Stress Assessment
Cited 13 times
Assessment of superoxide anion (O2.-) generation. Superoxide anion generation was determined by a standard assay.48 (link) Briefly, 0.1 µg/ml of PMA (Sigma), a potent macrophage stimulant, and 0.12 mM horse heart cytochrome-c (Sigma) were added to isolated cell suspensions after treatment schedule, and washing with PBS. Cytochrome-c reduction by generated superoxide was then determined by spectrophotometric absorbance at a 550 nm wavelength. Results are expressed n mol of cytochrome-c reduced/min, using extinction-coefficient 2.1 × 104 M−1 cm−1.
NADPH oxidase activity. After the treatment schedule, the macrophages of different groups prewarmed in Krebs ringer buffer (KRB) with 10 mM glucose at 37°C for 3 min. PMA (0.1 µg/ml) prewarmed at 37°C for 5 min was added, and the reaction was stopped by putting in ice. Centrifugation was carried out at 400 g for 5 min and the resultant pellet was resuspended in 0.34 M sucrose. The cells were then lysed with hypotonic lysis buffer. Centrifugation was carried out at 800 xg for 10 min and the supernatant used to determine enzyme activity. NADPH oxidase activity was determined spectrophotometrically by measuring cytochrome c reduction at 550 nm. The reaction mixture contained 10 mM phosphate buffer (pH 7.2), 100 mM NaCl, 1 mM MgCl2, 80 µM cytochrome c, 2 mM NaN3 and 100 µl of supernatant (final volume 1.0 ml). A suitable amount of NADPH (10–20 µl) was added last to initiate the reaction.49 (link)
Myeloperoxidase (MPO) activity. 200 µl of cell lysate was reacted with 200 µl substrate (containing H2O2 and OPD) in dark for 30 min. The blank was prepared with citrate phosphate buffer (pH 5.2) and substrate, in absence of cell free supernatant. The reaction was stopped with addition of 100 µl 2(N) sulfuric acid and reading was taken at 492 nm in a spectrophotometer.50
Determination of lipid peroxidation (MDA). Lipid peroxidation was estimated by the method of Ohkawa et al. in cell lysate.51 (link) Briefly, the reaction mixture contained Tris-HCl buffer (50 mM, pH 7.4), tert-butyl hydroperoxide (BHP) (500 µM in ethanol) and 1 mM FeSO4. After incubating the samples at 37°C for 90 min, the reaction was stopped by adding 0.2 ml of 8% sodium dodecyl sulfate (SDS) followed by 1.5 ml of 20% acetic acid (pH 3.5). The amount of malondialdehyde (MDA) formed during incubation was estimated by adding 1.5 ml of 0.8% TBA and further heating the mixture at 95°C for 45 min. After cooling, samples were centrifuged, and the TBA reactive substances (TBARS) were measured in supernatants at 532 nm by using 1.53 × 105 M−1 cm−1 as extinction coefficient. The levels of lipid peroxidation were expressed in terms of n mol/mg protein.
Protein carbonyls contents (PC). Protein oxidation was monitored by measuring protein carbonyl contents by derivatization with 2, 4-dinitrophenyl hydrazine (DNPH).52 (link) In general, cell lysate proteins in 50 mM potassium phosphate buffer, pH 7.4, were derivatized with DNPH (21% in 2 N HCl). Blank samples were mixed with 2 N HCl incubated at 1 h in the dark; protein was precipitated with 20% trichloro acetic acid (TCA). Underivatized proteins were washed with an ethanol:ethyl acetate mixture (1:1). Final pellets of protein were dissolved in 6.0 N guanidine hydrochloride and absorbance was measured at 370 nm. Protein carbonyls content was expressed in terms of µ mol/mg protein.
Activity of super oxide dismutase (SOD). SOD activity was determined from its ability to inhibit the auto-oxidation of pyrogalol according to Mestro Del and McDonald.53 The reaction mixture considered of 50 mM Tris (hydroxymethyl) amino methane (pH 8.2), 1 mM diethylenetriamine penta acetic acid, and 20–50 µl of cell lysate. The reaction was initiated by addition of 0.2 mM pyrogalol, and the absorbance measured kinetically at 420 nm at 25°C for 3 min. SOD activity was expressed as unit/mg protein.
Activity of catalase (CAT). Catalase activity was measured in the cell lysate by the method of Luck.54 The final reaction volume of 3 ml contained 0.05 M Tris-buffer, 5 mM EDTA (pH 7.0), and 10 mM H2O2 (in 0.1 M potassium phosphate buffer, pH 7.0). About 50 µl aliquot of the cell lysates were added to the above mixture. The rate of change of absorbance per min at 240 nm was recorded. Catalase activity was calculated by using the molar extinction coefficient of 43.6 M−1 cm−1 for H2O2. The level of CAT was expressed in terms of m mol H2O2 consumed/min/mg protein.
Determination of reduced glutathione (GSH). Reduced glutathione estimation in the cell lysate was performed by the method of Moron et al.55 (link) The required amount of the cell lysate was mixed with 25% of trichloroacetic acid and centrifuged at 2,000 xg for 15 min to settle the precipitated proteins. The supernatant was aspirated and diluted to 1 ml with 0.2 M sodium phosphate buffer (pH 8.0). Later, 2 ml of 0.6 mM DTNB was added. After 10 minutes the optical density of the yellow-colored complex formed by the reaction of GSH and DTNB (Ellman's reagent) was measured at 405 nm. A standard curve was obtained with standard reduced glutathione. The levels of GSH were expressed as µg of GSH/mg protein.
Oxidized glutathione level (GSSG). The oxidized glutathione level was measured after derevatization of GSH with 2-vinylpyidine according to the method of Griffith.56 (link) In brief, with 0.5 ml cell lysate, 2 µl 2-vinylpyidine was added and incubates for 1 hr at 37°C. Then the mixture was deprotenized with 4% sulfosalicylic acid and centrifuged at 1,000 xg for 10 min to settle the precipitated proteins. The supernatant was aspirated and GSSG level was estimated with the reaction of DTNB at 412 nm in spectrophotometer and calculated with standard GSSG curve.
Redox ratio (GSH/GSSG). Redox ratio was determined for all the seven groups by taking the ratio of reduced glutathione/oxidized glutathione.
Activity of glutathione peroxidase (GPx). The GPx activity was measured by the method of Paglia and Valentine.57 (link) The reaction mixture contained 50 mM potassium phosphate buffer (pH 7.0), 1 mM EDTA, 1 mM sodium azide, 0.2 mM NADPH, 1 U glutathione reductase and 1 mM reduced glutathione. The sample, after its addition, was allowed to equilibrate for 5 min at 25°C. The reaction was initiated by adding 0.1 ml of 2.5 mM H2O2. Absorbance at 340 nm was recorded for 5 min. Values were expressed as n mol of NADPH oxidized to NADP by using the extinction coefficient of 6.2 × 103 M−1 cm−1 at 340 nm. The activity of GPx was expressed in terms of n mol NADPH consumed/min/mg protein.
Activity of glutathione reductase (GR). The GR activity was measured by the method of Miwa.58 The tubes for enzyme assay were incubated at 37°C and contained 2.0 ml of 9 mM GSSG, 0.02 ml of 12 mM NADPH, Na4, 2.68 ml of 1/15 M phosphate buffer (pH 6.6) and 0.1 ml of cell lysate. The activity of this enzyme was determined by monitoring the decrease in absorbance at 340 nm. The activity of GR was expressed in terms of n mol NADPH consumed/min/mg protein.
Activity of glutathione-s-transferase (GST). The activity of GST activity was measured by the method of Habig et al.59 (link) The tubes of enzyme assay were incubated at 25°C and contained 2.85 ml of 0.1 M potassium phosphate (pH 6.5) containing 1 mM of GSH, 0.05 ml of 60 mM 1-chloro-2, 4-dinitrobengene and 0.1 ml cell lysate. The activity of this enzyme was determined by monitoring the increase in absorbance at 340 nm.
Protein estimation. Protein was determined according to Lowry et al. using bovine serum albumin as standard.60
Mahapatra S.K., Chakraborty S.P., Das S, & Roy S. (2009). Methanol extract of Ocimum gratissimum protects murine peritoneal macrophages from nicotine toxicity by decreasing free radical generation, lipid and protein damage and enhances antioxidant protection. Oxidative Medicine and Cellular Longevity, 2(4), 222-230.
Publication 2009
3
Quantifying Tissue Glutathione Levels
Cited 11 times
Frozen tissue was weighed on ice and rapidly homogenized in ice cold 3% sulfosalicylic acid (SSA) containing 0.1mM EDTA with a PowerGen Model 125 blade-type homogenizer to yield a 10% (w/v) homogenate. 200 μL of this homogenate was immediately transferred to 1 mL of a 10 mM NEM solution prepared in 100 mM potassium phosphate buffer on ice. Another aliquot of the homogenate was diluted 1:50 in 0.01 N HCl in H2O for use in determination of total glutathione. Tubes were then centrifuged at 4°C, 14,000 × g, for 4 minutes and the deproteinized supernatants were transferred to fresh tubes. All samples were kept on ice. Removal of excess NEM was accomplished by chromatographic separation using a small C18 column (Sep-Pak; Waters Associates, Millipore Corporation, Milford, PA). 700 μL of sample was passed through the column (~1 drop/sec) by injection and into a fresh tube, followed by 1 mL of 100 mM potassium phosphate buffer. Regeneration of the column for use with subsequent samples was accomplished with a 6 mL methanol rinse using a fresh syringe. To prevent interference due to methanol in the enzymatic assay, the column was air dried using the same syringe, rinsed with H2O, and air dried again, before applying the next sample. In all, the process required < 5 minutes per sample. Between experiments, the C18 cartridges were stored in methanol. Determination of GSSG using 2VP as the GSH masking agent was done as described (Griffith, 1980 (link)), in parallel with the above experiments. Briefly, 200 μL of the deproteinized supernatant was mixed with 4 μL 2VP and 12 μL triethanolamine (to pH 7.0–7.5) and incubated at room temperature for 1 h. Following the 1 h incubation, 2VP treated samples were diluted 1:30 in 100 mM potassium phosphate buffer. GSH sample supernatants in HCl were further diluted 1:26 in 100 mM potassium phosphate before measurement. NEM treated samples were used without further dilution.
McGill M.R, & Jaeschke H. (2015). A direct comparison of methods used to measure oxidized glutathione in biological samples: 2-vinylpyridine and N-ethylmaleimide. Toxicology mechanisms and methods, 25(8), 589-595.
Publication 2015
Buffers Chromatography Cold Temperature Edetic Acid Enzyme Assays Freezing Glutathione Disulfide Methanol potassium phosphate Regeneration sulfosalicylic acid Syringes Technique, Dilution Tissues triethanolamine
4
Hepatic Cytochrome b5 Null Mice: A Versatile Model for Drug Metabolism Studies
Cited 8 times
Chemicals—All reagents unless stated were purchased from
Sigma. NADPH was obtained from Melford Laboratories (Ipswich, UK). Bufuralol,
1′-hydroxybufuralol, 7-benzyloxy-4-trifluoromethylcoumarin (BFC),
7-methoxy-4-trifluoromethylcoumarin (MFC),
7-hydroxy-4-trifluoromethylcoumarin, and hydroxytolbutamide were purchased
from BD Gentest (Cowley, UK). Midazolam, 1-hydroxymidazolam, and
4-hydroxymidazolam were kind gifts from Roche Applied Science, and
1-hydroxymetoprolol and O-demethylmetoprolol were generous gifts from
Astra Häsle (Mölndal, Sweden).
Generation of Hepatic Microsomal Cytochrome b5 Null
Mice—A targeting vector was constructed from an 18-kb DNA fragment,
produced by fusing overlapping PCR fragments generated from mouse 129/Ola
genomic DNA (supplemental Fig. 1A), containing exons 2–5 of the
mouse cytochrome b5 gene. A cassette, flanked by same
orientation loxP sites and containing a selectable marker (neomycin),
driven by the herpes simplex thymidine kinase promoter, was cloned into a BclI
site in intron 1, and a third loxP site was cloned into a KpnI site
in intron 5. The construct was checked by PCR and sequencing and transfected
into GK129/1 embryonic stem cells by electroporation; the embryonic stem cells
were subsequently cultured in 96-well plates under G418 selection.
G418-resistant clones were screened for specific homologous recombination by
Southern blot analysis, using BglII and an 800-bp PCR fragment generated using
5′-GGCACAACACCAATTATTTGTC-3′ and
5′-GACAGTCCTTAACACAAGCTC-3′ as forward and reverse primers,
respectively. Two correctly targeted embryonic stem cell clones (Cytb+/lox5) were expanded, injected into
C57BL/6 blastocysts, and transferred into pseudopregnant mice. Male chimeric
mice were bred to C57BL/6 mice, and heterozygous offspring were screened by
Southern blot and multiplex PCR to confirm germ line transmission of the
Cytb +/lox5 genotype
(supplemental Fig. 1B) using the following primer set: 1) forward
primer, 5′-CCAATGGTCTCTCCTTGGTC-3′;2) lox/neomycin
reverse primer, 5′-CAATAGCAGCCAGTCCCTTC-3′; 3) wild-type reverse
primer, 5′-GATGGAGTTCCCCGATGAT-3′.
Mouse Breeding and
Maintenance—Cytb5lox/+ mice were crossed to produce homozygous
Cytb5lox/lox mice and maintained by
random breeding on a 129P2 × C57BL/6 genetic background.
Cytb5lox/lox mice were crossed with a
transgenic mouse line expressing Cre recombinase under the control of the
hepatocyte-specific rat albumin promoter (CreALB)
(22 (link)) on a C57BL/6 background,
and
Cytb5lox/+::CreALB offspring were backcrossed with
Cytb5lox/lox mice to generate
liver-specific microsomal cytochrome b5 conditional
knock-out mice (HBN;
Cytb5lox/lox::CreALB) and
control (wild-type, Cytb5lox/lox)
mice. The HBN line was thereafter maintained by random intercrossing of these
two lines. The presence of the CreALB transgene was determined as
previously described (23 (link)).
All mice were maintained under standard animal house conditions, with free
access to food and water, and a 12-h light/12-h dark cycle. All animal work
was carried out on male 10-week-old mice in accordance with the Animal
Scientific Procedures Act (1986) and after local ethical review.
In Vivo Drug Treatments—HBN and wild-type mice were
administered the following drugs either concomitantly as a mixture or
individually: chlorzoxazone (5 mg/kg), metoprolol (2 mg/kg), midazolam (5
mg/kg), phenacetin (5 mg/kg), and tolbutamide (5 mg/kg), dissolved in mixture
buffer (5% ethanol, 5% DMSO, 35% polyethylene glycol 200, 40% phosphate
buffered saline, and 15% water), by intravenous injection or orally by
gavage.
Preparation of Microsomes—Microsomes were prepared from
wild-type and HBN mouse tissues, using 0.3–0.5 g of tissue, by a
modified method of Meehan et al. (24 (link)), using sonication instead
of mechanical homogenization
(25 (link)). Microsomal protein
concentrations were determined using the Bio-Rad protein assay reagent. POR
activity was estimated by NADPH-dependent cytochrome c reduction
(26 (link)). Microsomes were stored
at –70 °C until required.
Immunoblotting—Western blot analysis was carried out as
previously described using polyclonal antisera raised against human POR
(27 (link)); rat cytochrome
b5; rat CYP2A1, CYP2B1, CYP2C6, CYP3A1, and CYP4A1
(28 (link)); or human full-length
CYP2A4, CYP2D6, and CYP2E1
(25 (link),
29 (link)). Polyclonal antiserum to
rat cytochrome b5 reductase and a monoclonal antibody
raised against rat CYP1A1 were also
used.3 The polyclonal
antiserum to cytochrome b5 oxidoreductase was a kind gift
from Dr. Hao Zhu (Kansas University Medical Center, Kansas City, KS).
Immunoreactive proteins were detected using polyclonal goat anti-rabbit,
anti-mouse, or anti-sheep horseradish peroxidase immunoglobulins as secondary
antibodies (Dako, Ely, UK) and visualized using Immobilon™
chemiluminescent horseradish peroxidase substrate (Millipore, Watford, UK) and
a FUJIFILM LAS-3000 mini-imaging system (Fujifilm UK Ltd.). Densitometric
analysis was performed using Multi Gauge version 2.2 software (Fujifilm UK
Ltd.).
Generic Microsomal Incubations—Microsomal incubations were
carried out in triplicate in 50 mm Hepes, pH 7.4, 30 mm MgCl2 containing mouse liver microsomes and substrate prewarmed to
37 °C before initiation of the reaction by the addition of either NADPH or
NADH to a final concentration of 0.5 or 1 mm, respectively.
Fluorogenic Assay Incubations—Assays were performed in a
final volume of 150 μl using white 96-well plates and the following
substrate and microsome concentrations: BFC, 50 μm substrate, 20
μg of mouse liver microsomes; EFC, 40 μm substrate, 15 μg
of mouse liver microsomes; MFC, 180 μm of substrate, 15 μg of
mouse liver microsomes; ethoxyresorufin (ER) and benzoxyresorufin (BR), 1
μm substrate, 11.25 μg of mouse liver microsomes. Reactions
were measured in real time for 3 min, using the recommended excitation and
emission wavelengths for each probe using a Fluroskan Ascent FL plate reading
fluorimeter (Labsystems, UK). Turnover rates were calculated using authentic
metabolite standards (7-hydroxy-4-trifluoromethylcoumarin for BFC, EFC, and
MFC assays and resorufin for ER and BR assays).
NADH-mediated Incubations for HPLC or Liquid Chromatography-Tandem Mass
Spectrometry (LC-MS/MS) Analysis—NADH-mediated reactions were
performed in triplicate using the following conditions: bufuralol, 300
μm (final concentration), 20 μg of mouse liver microsomes in
a final volume of 150 μl for 6 min; chlorzoxazone, 1 mm (final
concentration) and 20 μg of mouse liver microsomes in a final volume of 150
μl for 15 min; midazolam, 50 μm (final concentration) and 25
μgof mouse liver microsomes in a final volume of 150 μl for 9 min;
metoprolol, 800 μm (final concentration) and 30 μg of mouse
liver microsomes in a final volume of 150 μl for 60 min; phenacetin, 200
μm (final concentration) and 20 μg of mouse liver microsomes
in a final volume of 100 μl for 9 min; tolbutamide, 800 μm (final concentration) and 30 μg of mouse liver microsomes in a final volume
of 150 μl for 60 min. Assays were stopped by the addition of either 0.5
assay volumes (for bufuralol, chlorzoxazone, and tolbutamide assays) or 1
assay volume (for midazolam and phenacetin assays) of ice-cold methanol and
incubated on ice for 10 min.
Kinetic Determinations—Assays to determine the apparent
kinetic parameters were performed in triplicate with wild-type and HBN liver
microsomes under conditions of linearity for time and protein (data not shown)
using the same buffer/NADPH conditions as described above, with the following
concentrations of substrates: chlorzoxazone, 10–1000 μm;
phenacetin, 1.7–150 μm; midazolam, 0.9–75
μm; metoprolol, 10–1000 μm; tolbutamide,
10–1000 μm (12 concentration points/determination).
Metabolites were detected by LC-MS/MS as described in the supplemental
materials. The data generated were analyzed by nonlinear regression using the
Michaelis-Menten equation (chlorzoxazone, phenacetin, midazolam, and
metoprolol), whereas the Hill equation (tolbutamide)
(Equation 1) was used to
determine the kinetic parameters Vmax,S50, and
the Hill coefficient (n).

In Vivo Pharmacokinetics—Whole blood (10 μl) was taken
from the tail vein at intervals after drug administration and transferred into
a tube containing heparin (10 μl, 15 IU/ml). Internal standard solution (10
μl; 500 ng of caffeine and 500 ng of resorpine) was added to each tube.
Protein precipitation was carried out by adding methanol (75 μl), followed
by 8% sulfosalicylic acid (55 μl). Samples were mixed for 1 min and
centrifuged at 13,000 rpm for 5 min, and the supernatant was analyzed by
HPLC.
The range of concentrations for the standard curves was constructed for
quantifying blood levels by spiking blank blood samples with known amounts of
chlorzoxazone, metoprolol, midazolam, phenacetin, and tolbutamide. Extraction
and protein precipitation were carried out as outlined above for the test
samples.
Analysis of in Vitro and in Vivo Data—Average rates of
metabolism were calculated for each triplicate incubation of mouse liver
microsomes from each genotype (n = 6), and these data were then used
to calculate p values using an unpaired t test (available on
the World Wide Web). Pharmacokinetic parameters were calculated using
WinNonLin software, version 3.1. A simple noncompartmental model was used to
calculate area under the curve (AUC), terminal half-life, maximum plasma
concentration (Cmax), and clearance. Details of assays and
separation conditions for HPLC and LC-MS/MS are given in the supplemental
materials.
Finn R.D., McLaughlin L.A., Ronseaux S., Rosewell I., Houston J.B., Henderson C.J, & Wolf C.R. (2008). Defining the in Vivo Role for Cytochrome b5 in Cytochrome P450 Function through the Conditional Hepatic Deletion of Microsomal Cytochrome b5. The Journal of Biological Chemistry, 283(46), 31385-31393.
Publication 2008
5
Protein Glutathionylation in OVCAR-3 Cells
Cited 7 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2008
Cell Lines Cells Culture Media Kidney Monkeys Pellets, Drug Penicillins Proteins Staphylococcal Protein A Streptomycin Sulfhydryl Compounds sulfosalicylic acid

Most recents protocols related to «Sulfosalicylic acid»

1
Quantifying Proline in Leaf Samples
Not available on PMC !
The determination of proline content started with the homogenization of 0.3 g leaf samples taken from the forth stipule in liquid nitrogen, followed by dissolution in 1 ml of 3% sulfosalicylic acid (Bates, et al., 1973) . Then, 0.1 ml of the sample, after centrifugation, was mixed with 0.2 ml acid ninhydrin, 0.2 ml of 96% acetic acid, and 0.1 ml of 3% sulfosalicylic acid. The mixtures were held at 96°C for 1 hour, and after centrifugation and mixing with 1 ml of toluene, the absorbance of the upper phase was read at 520 nm.
Akçay U.Ç., Kumbul H.N., & Erkan İ.E. (2024). Salicylic acid improves cold and freezing tolerance in pea. Harran Tarım ve Gıda Bilimleri Dergisi.
Publication 2024
2
Amino Acid Quantification in Biofluids
Not available on PMC !
An aliquot of 20µL of urine was mixed with 130µL of methanol containing 4.8mg/mL 5-sulfosalicylic acid dihydrate and 0.1µg/mL of d3-α-AAA and d9-PA as the internal standards. An aliquot of 20µL of plasma was mixed with 180µL of methanol containing 3.5mg/mL 5-sulfosalicylic acid dihydrate and 0.16µg/mL of d3-α-AAA and d9-PA as the internal standard. Three DBS (ID 3 mm) was mixed with 150µL of 70% methanol containing 3mg/mL 5-sulfosalicylic acid dihydrate, 0.1% formic acid and 0.1µg/mL of d3-α-AAA and d9-PA as the internal standard. DUS specimens were prepared as the urine after reconstituted by water. The mixture was vortexed for 20-30 min, allowed to stand for 3 min, and then centrifuged at 20000g at 4°C for 10min. An aliquot of supernatant was transferred to a clean tube and dried by nitrogen ow in RT. The residue was derivatized with 50µl of 3N HCl in n-butanol (v/v) at 65°C and 600 rpm for 20 min dried as described above and reconstituted in 100µL water/methanol (70:30) containing 0.1% of formic acid.
Jiao X., Gong P., Niu Y., Xu Z., Zhou Z., Qin J., & Yang Z. (2024). Evaluating the suitability of 6-oxo-PIP as a novel biomarker for pyridoxine-dependent epilepsy in multiple samples.
Publication 2024
3
Evaluating Manganese Stress Responses
The physiological indicators of the old leaves dealt with varying Mn concentrations (5, 35, 100, 165, and 230 µM) were assessed as follows: (1) Activity of SOD was determined using the NBT (nitrogen blue tetrazole) technique [70 (link)]. (2) Activity of POD was determined utilizing the (CH3O)C6H4OH (guaiacol) technique [71 (link)]. (3) APX activity was measured employing the sulfosalicylic acid method [72 (link)]. (4) CAT activity was assessed via spectrophotometry [73 (link)]. (5) Proline content was quantified using the sulfosalicylic acid method [72 (link)]. (6) MDA content was measured utilizing the thiobarbituric acid method [74 (link)].
Pan Y., Shi J., Li J., Zhang R., Xue Y, & Liu Y. (2024). Regulatory Mechanism through Which Old Soybean Leaves Respond to Mn Toxicity Stress. International Journal of Molecular Sciences, 25(10), 5341.
Full text: Click here
Publication 2024
4
Proline and MDA Content Determination
Proline content was determined using sulfosalicylic acid, and MDA content was determined using the chromogenic thiobarbituric acid TBA method described by Kumar [57 (link)].
Qiu H., Sun C., Dormatey R., Bai J., Bi Z., Liu Y., Liu Z., Wei J., Mao S, & Yao P. (2024). Thiamethoxam Application Improves Yield and Drought Resistance of Potatoes (Solanum tuberosum L.). Plants, 13(4), 477.
Full text: Click here
Publication 2024
5
Quantifying Leaf Biochemical Parameters
Not available on PMC !
Proline concentration in leaves was determined using the sulfosalicylic acid method described by Zheng et al. [20] (link), where 5 mL of reaction solution consisted of 1 mL of 3% sulfosalicylic acid leaf extract, 1 mL of glacial acetic acid, 1 mL of acidic ninhydrin reagent, and 2 mL of toluene. Hydrogen peroxide (H 2 O 2 ) levels in leaves were measured as per the protocol described by Velikova et al. [21] (link), where the reaction solution consisted of 1 mL of 0.1% trichloroacetic acid leaf extract, 1 mL of 10 mmol/L potassium phosphate buffer (pH 7.0), and 2 mL of 1 mol/L potassium iodide solution. Leaf soluble protein levels were analyzed by the Coomassie Brilliant Blue G250 staining method outlined by Bradford [22] (link).
Wen Y., Zhou L., Xu Y., Allah E.F.A., Allah E.F.A., & Wu Q. (2024). Growth Performance and Osmolyte Regulation of Drought-Stressed Walnut Plants Are Improved by Mycorrhiza. Agriculture, 14(3), 367-367.
Publication 2024

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Gssg gsh quantification kit by Dojindo Laboratories
Sourced in Japan, United States, China
The GSSG/GSH Quantification Kit is a laboratory tool designed to measure the levels of glutathione disulfide (GSSG) and reduced glutathione (GSH) in samples. The kit provides a rapid and accurate method for quantifying these important cellular antioxidants. It is intended for use in research and scientific applications.
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Glutathione reductase by Merck Group
Sourced in United States, Germany, Spain, India, Sao Tome and Principe
Glutathione reductase is an enzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH). This enzyme is involved in maintaining the balance of reduced and oxidized glutathione within cells, which is important for cellular antioxidant defense systems.
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2 vinylpyridine by Merck Group
Sourced in United States
2-vinylpyridine is a chemical compound used in various laboratory applications. It is a clear, colorless liquid with a characteristic odor. The core function of 2-vinylpyridine is as a reagent and monomer for the synthesis of polymers and copolymers, which can be utilized in a range of research and industrial processes.
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Nadph by Merck Group
Sourced in United States, Germany, Sao Tome and Principe, China, United Kingdom, France, Czechia, Spain, India, Italy, Canada, Macao, Japan, Portugal, Brazil, Belgium
NADPH, or Nicotinamide Adenine Dinucleotide Phosphate, is a cofactor essential for various cellular processes. It plays a crucial role in enzymatic reactions, serving as an electron donor in oxidation-reduction reactions. NADPH is a key component in several metabolic pathways, including biosynthesis, antioxidant defense, and energy production.
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L 8800 by Hitachi
Sourced in Japan
The L-8800 is a high-performance UV-Vis spectrophotometer developed by Hitachi. It is designed to accurately measure the absorbance of samples across a wide range of wavelengths in the ultraviolet and visible light spectrum.
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Bovine serum albumin (bsa) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico
Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

More about "Sulfosalicylic acid"

Sulfosalicylic acid (SSA) is a versatile chemical compound that has a wide range of research applications.
It is also known as 5-sulfosalicylic acid, and it can be used in various analytical techniques, including protein analysis, microalbuminuria detection, and as a precipitating agent.
SSA is a white crystalline solid with a melting point of approximately 202°C.
It is soluble in water and has a pKa value of 2.85, making it a useful reagent for acidic conditions.
Researchers can utilize PubCompare.ai's AI-driven platform to efficiently locate and compare published protocols for working with SSA, identifying the best solutions to optimize their research workflows.
SSA is commonly used in glutathione assays, such as the Glutathione Assay Kit and the GSSG/GSH Quantification Kit.
These assays rely on the ability of SSA to precipitate proteins, allowing the quantification of reduced glutathione (GSH) and oxidized glutathione (GSSG) levels.
Glutathione reductase, an enzyme that catalyzes the conversion of GSSG to GSH, is also an important component in these assays.
In addition to its use in protein and glutathione analysis, SSA can also be used as a precipitating agent for bovine serum albumin (BSA) and other proteins.
The 2-vinylpyridine compound is sometimes used in conjunction with SSA to mask interfering substances in these protein precipitation procedures.
PubCompare.ai's AI-driven platform can be a valuable tool for researchers working with SSA, as it helps them efficiently locate and compare published protocols from the literature, preprints, and patents.
This allows them to identify the best solutions and optimize their research workflows, ultimately enhancing the efficiency and productivity of their studies.