Ammonium ferrous sulfate is a chemical compound with the formula (NH4)2Fe(SO4)2.
It is a crystalline salt that is used in various applications, including as a fertilizer, an oxidizing agent, and a reducing agent.
Ammonium ferrous sulfate is also known for its use in the treatment of iron deficiency anemia.
Its chemical structure consists of ammonium (NH4+) and ferrous (Fe2+) ions, along with sulfate (SO4(2-)) ions.
This inorganic compound has a green or violet color and is soluble in water.
Reseachers may use ammonium ferrous sulfate in their studies, for example, to investigate its potential applications or to understand its chemical properties and behavior.
Most cited protocols related to «Ammonium ferrous sulfate»
This activity was determined according to a previously described method [13 (link)] with minor changes. An aliquot of 50 mM H2O2 and various concentrations (0–2 mg/ml) of samples were mixed (1:1 v/v) and incubated for 30 min at room temperature. After incubation, 90 μl of the H2O2-sample solution was mixed with 10 μl HPLC-grade methanol and 0.9 ml FOX reagent was added (prepared in advance by mixing 9 volumes of 4.4 mM BHT in HPLC-grade methanol with 1 volume of 1 mM xylenol orange and 2.56 mM ammonium ferrous sulfate in 0.25 M H2SO4). The reaction mixture was then vortexed and incubated at room temperature for 30 min. The absorbance of the ferric-xylenol orange complex was measured at 560 nm. All tests were carried out six times and sodium pyruvate was used as the reference compound [14 (link)].
Hazra B., Biswas S, & Mandal N. (2008). Antioxidant and free radical scavenging activity of Spondias pinnata. BMC Complementary and Alternative Medicine, 8, 63.
Hydrogen peroxide extraction was carried out according to Veljovic-Jovanovic et al. (2002) (link). Briefly, 100 mg of stem from the top, middle, and bottom part of tomato seedlings was harvested, snap-frozen in liquid nitrogen and analyzed immediately. Samples were homogenized in 1.5 mL 1 M HClO4 with 100 mg of insoluble polyvinylpyrrolidone, which can remove phenolic compounds. Homogenates were centrifuged at 13000 × g for 10 min at 4°C. The H2O2 content in the supernatant was then determined as described by Cheeseman (2006) (link). Briefly, 60 μL extract was mixed with 600 μL eFOX reagents (containing 250 μM ferrous ammonium sulfate, 100 μM sorbitol, 100 μM xylenol orange, and 1% ethanol in 25 mM H2SO4). Then, the difference in absorbance between 550 and 800 nm was recorded at least 30 min after mixing the supernatant with the eFOX reagents. The content of H2O2 was calculated using a standard curve of H2O2.
Liu Y.H., Offler C.E, & Ruan Y.L. (2014). A simple, rapid, and reliable protocol to localize hydrogen peroxide in large plant organs by DAB-mediated tissue printing. Frontiers in Plant Science, 5, 745.
The soil moisture content was measured at monthly interval during 2015. Three random soil samples at depths 0–10, 10–20, and 20–40 cm, respectively, were collected. The individual soil samples were then placed in sterile plastic sealing bags and transported to the laboratory, where they were oven-dried at 105°C for 8 h and used for further analysis. Two-years after mulching, the soil was sampled from the tree pits on June 26, 2016. Three soil samples per tree pit at depths 0–10, 10–20, and 20–40, respectively, were collected in 100 cm3 volumetric containers and used to evaluate the physical properties of soil. Further, six random soil samples at depths 0–10, 10–20, and 20–40 cm were collected to evaluate the chemical properties of soil. All the soil samples were placed in sterile plastic sealing bags and transported to the laboratory in car refrigerators. The soil sample used to evaluate the chemical properties was divided into three subsamples. The first subsample was stored at 4°C to analyze the moisture content. The second subsample was air-dried in a soil drying room and ground. The sample was then passed through a 2-mm sieve to remove pebbles, construction wastes, fine roots, and other foreign materials before the analyses. The third subsample was obtained by passing a portion of the second subsample through a 0.149-mm sieve. The bulk density of the sampled soil was measured as the mass of oven-dried soil. The total porosity was assessed by measuring soil saturation (total volume of water-filled soil pores); microporosity was assessed using tension table and water column of 6 × 10−3 MPa; macroporosity was calculated as the difference between the total porosity and microporosity. All evaluations were performed according to the methodologies described by Embrapa (1997) [28 ].The second subsample of soil was used to determine the mineral nitrogen (N) content and pH. The mineral N was determined by alkali-hydrolytic diffusion method [29 ]. The soil pH was determined using a pH meter at a soil to water ratio of 2:5. The third subsample was used to estimate organic matter, available phosphorus (P), available potassium (K), and total N. The organic matter was measured by sulfuric acid-potassium dichromate wet oxidation, followed by titration with ferrous sulfate according to the procedure of Walkley-Black [30 ]. The available P in the soil was measured by the Olsen method. The available K in the soil was determined using a flame photometer after ammonium acetate extraction.
Qu B., Liu Y., Sun X., Li S., Wang X., Xiong K., Yun B, & Zhang H. (2019). Effect of various mulches on soil physico—Chemical properties and tree growth (Sophora japonica) in urban tree pits. PLoS ONE, 14(2), e0210777.
Cloning and Expression of Ferritin Polypeptides—cDNAs containing the sequence of human WT-FTL and human mutant FTL498–499InsTC were introduced into the pET-28a(+) expression vector (Novagen, EMD Chemicals Inc.). The cDNAs were cloned between the BamHI and XhoI sites, downstream from and in-frame with the sequence encoding an N-terminal His6 tag. To eliminate the His6 tag (included in the expression vector), the sequence of the vector was modified by introducing the recognition sequence for cleavage by factor Xa before the coding sequence of the ferritin genes. PCR amplification of the ferritin cDNAs was performed using the upstream primer F1 5′-TGG ATC CAT CGA AGG TCG TAT GAG CTC CCA GAT T-3′ and the downstream primer R1 5′-TTA TGC CTC GAG CCC TAT TAC TTT GCA AGG-3′. F1 contains the factor Xa sequence (underlined). pET-28a(+) carrying WT-FTL and MT-FTL cDNAs was transformed into BL21 (DE3) Escherichia coli (Invitrogen). Transformed cells were grown in Luria broth medium (LB) containing 30 μg/ml kanamycin (Invitrogen) at 37 °C up to an absorbance of 0.9–1.0 at 600 nm. Bacteria were induced to overexpress recombinant proteins by adding 1 mm isopropyl thio-β-d-galactopyranoside (ICN Biotechnologies) for 12 h at 25 °C. Purification of Recombinant WT- and MT-FTL Homopolymers—Cells were harvested by centrifugation and frozen at -80 °C. The cell pellets were suspended in 50 mm sodium phosphate, 500 mm NaCl (pH 7.4), 1 mg/ml lysozyme, and a protease inhibitor mixture (Complete, Roche Applied Science) for 30 min. Bacteria were disrupted by sonication, and the insoluble material was removed by centrifugation at 21,000 × g for 30 min. The soluble fraction was purified by nickel iminodiacetic acid affinity chromatography using an AKTA purifier system (GE Healthcare). Purified protein was eluted with 250 mm imidazole in 50 mm sodium phosphate (pH 7.4), 0.5 m NaCl. Recombinant proteins were diluted with 50 mm Tris and 10% glycerol (v/v) down to an absorbance of 0.5 at 280 nm, and ferritins were cleaved from the His tag by digestion with factor Xa protease (GE Healthcare) (5 units/mg of protein). After being dialyzed against 50 mm Tris, pH 8.0, for 18 h, proteins were further purified by anion exchange chromatography (Mono Q) using a linear NaCl elution gradient in 50 mm Tris (pH 8). Peak fractions were ∼95% pure based on SDS-12% PAGE (Pierce) and Coomassie Blue staining. The efficiency of tag removal was confirmed by N-terminal protein sequencing analysis, and the molecular weight of the recombinant proteins was determined by matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Protein concentration was determined using the BCA reagent (Pierce) with bovine serum albumin as standard. Gel Filtration Chromatography—Size exclusion chromatography was performed on a Superose 6 10/300 GL column (GE Healthcare) equilibrated with 50 mm Tris, 150 mm NaCl (pH 7.4) using an AKTA purifier. The column was calibrated with gel filtration standards (GE Healthcare). Fractions were detected photometrically, and peak areas and kav values were evaluated using the UNICORN 5.1 software (GE Healthcare). All gel filtration experiments were run at room temperature. Transmission Electron Microscopy (TEM)—Ferritins were fixed using the “single droplet” parafilm protocol. The specimens were dropped onto a 400-mesh carbon/Formvar-coated grid (Nanoprobes) and allowed to absorb to the Formvar for a minimum of 1 min. Excess fluid was removed using filter paper, and the unbound protein was washed, and the grids were placed on a 50-μl drop of Nanovan (Nanoprobes) with the section side downwards. Finally, the grids were dried, placed in the grid chamber, and stored in desiccators before the samples were observed with a Tecnai G2 12 Bio Twin (FEI) transmission electron microscope. Preparation of Apoferritins—Recombinant FTL homopolymers were treated for iron removal as described previously (14 (link)). Briefly, recombinant ferritins were incubated with 1% thioglycolic acid (pH 5.5) and 2,2′-bipyridine, followed by dialysis against 0.1 m phosphate buffer (pH 7.4). We consistently achieve less than five atoms of iron per ferritin 24-mer, as determined by the colorimetric ferrozine-based assay for the quantitation of iron (15 (link)). Iron Loading of Apoferritins—Freshly prepared ferrous ammonium sulfate (0.5–4.5 mm) in 10 mm HCl was added to MT- and WT-FTL apoferritin homopolymers (1 μm) in 0.1 m Hepes buffer (pH 7.4) at room temperature (16 (link)). After 2 h, the samples were centrifuged at 14,000 × g for 15 min. Iron incorporation was initially monitored by measuring absorbance of the supernatants at 310 nm (14 (link), 17 (link)). Iron incorporation into ferritin was more precisely determined by densitometric analysis of Prussian blue staining of supernatants run on nondenaturing gel electrophoresis. Pellets were analyzed by SDS-12% PAGE. Apoferritins were also incubated in a molar ratio 1:3500 with ferrous ammonium sulfate and centrifuged at 14,000 × g for 15 min. Pellets were resuspended in a solution containing 6 mm deferroxamine (DFX), 0.1 m Hepes (pH 7.4) and incubated for 2 h at 24 °C. After centrifugation, supernatants were analyzed by nondenaturing gel electrophoresis. Circular Dichroism Spectroscopy—CD spectra of recombinant apoferritin homopolymers were obtained in 50 mm phosphate buffer (pH 7.4) at 25 °C in a Jasco 810 spectropolarimeter (Jasco Corp.), using a protein concentration of 0.12 and 1.5 μm for far-UV and near-UV, respectively. Far-UV CD spectra were recorded in a 1.0-mm path length cell from 250 to 190 nm with a step size of 0.1 nm and a bandwidth of 1.0 nm. Each spectrum represents the mean of 15 scans. CD spectra of the buffer/cuvette were recorded and subtracted from the protein spectra before averaging. Secondary structure analyses were performed using DICHROWEB (18 (link), 19 ), which allows secondary structure analyses via the software package CDPro (20 (link)). SELCON3 (21 (link)), CONTINLL (22 (link)), and CDSSTR (23 (link)) programs were used for comparing variations in the amount of secondary structure between MT- and WT-FTL homopolymers. Normalized root mean square deviation values of < 0.1 for the three methods meant that the experimental and simulated spectra were in close agreement. Near-UV CD spectra were recorded in a 1.0-cm path length cell from 400 to 250 nm with a step size of 1.0 nm and a bandwidth of 1.5 nm. For all spectra, an average of five scans was obtained. Intrinsic Protein Fluorescence and Thermal Stability Studies of Homopolymers—Fluorescence spectra were recorded using a spectrofluorimeter (PerkinElmer Life Sciences) equipped with a Selecta Ultraterm water bath for temperature control. Apoferritin spectra were obtained with excitation at 280 and 295 nm with 1.5 μm protein in 1-cm path length cells and with 0.1 m phosphate (pH 7.4). Blanks without protein were subtracted from the spectra. Thermal denaturation was induced by increasing the temperature from 20 to 100 °C at a rate of 1 °C/min. To overcome the inherent difficulty in denaturing ferritin, these experiments were performed in 0.1 m phosphate buffer (pH 7.4) containing 4.0 m guanidine hydrochloride (GdnHCl). Homopolymer stability was monitored using the ratio of intrinsic fluorescence emission of 355 over 330 nm with excitation at 295 nm (24 (link), 25 (link)) with a maximum at 330 nm signifying native ferritin (mt and WT) and 355 nm, denatured ferritin. ANS Fluorescence and Binding Studies—Extrinsic fluorescence spectra were recorded using a spectrofluorimeter (PerkinElmer Life Sciences) in 1.0-cm cuvettes at 25 °C. ANS binding to apoferritin homopolymers was monitored through fluorescence enhancement with ANS excitation at 360 nm and emission recorded from 600 to 400 nm. MT-FTL apoferritins were prepared by diluting stock solutions to 1.5 μm in 0.05 m phosphate buffer (pH 7.4). Stock solutions of ANS (Invitrogen) were prepared in water, and the concentration was determined optically at 350 nm using an extinction coefficient of 4950 m-1 cm-1. ANS was added to the diluted ferritin samples and equilibrated for 30 min prior to the measurements, and spectra were background corrected. Binding of ANS to ferritin was quantitated by Scatchard analysis (26 ). Thermolysin Treatment of WT- and MT-FTL Apoferritin Homopolymers—Proteolysis of recombinant MT- and WT-FTL homopolymers was initiated by adding to 10 μg of ferritin a 10-fold concentrated stock solution (36.5 units/mg) of thermolysin (Fluka) in Hepes (0.1 m) (pH 7.0), 10 mm CaCl2 to a final concentration of 0.2 mg/ml. The reaction was stopped by the addition of EDTA (50 mm) and Laemmli sample buffer. Samples treated with thermolysin and controls without thermolysin were boiled and loaded onto SDS-polyacrylamide gels (4–20%) (Pierce). Gels were stained with Coomassie Blue (Total protein) or blotted against the C-terminal antibodies (MT-1283 or WT-1278) (9 (link)) or against the N-terminal antibody D18 (Santa Cruz Biotechnology, Inc), which recognized both polypeptides. Astrocyte Cell Cultures and Iron/Chelator Treatment—Primary cortical astrocyte cultures were prepared from 1-day-old mouse pups according to the procedures of Saneto and De Vellis (27 ) and Cassina et al. (28 (link)), with minor modifications. Pups were obtained from transgenic dams homozygous for the FTL498–499InsTC mutation in C57BL/6J genetic background (29 (link)). Briefly, cerebral cortices were removed, and the tissue was minced and dissociated in 0.25% trypsin (Invitrogen) for 15 min at 37 °C. Cells were collected by centrifugation and plated at a density of 2.0 × 106 cells in 25-cm2 flasks (Corning Glass) in Dulbecco's modified Eagle's medium supplemented with 10% fetal bovine serum, Hepes (25 mm), penicillin (100 IU/ml), and streptomycin (100 μg/ml) (Invitrogen). When confluent, cultures were shaken for 48 h at 250 rpm at 37 °C, incubated for another 48 h with 10 μm cytosine arabinoside, and then amplified to 2.5 × 104 cells/cm2 in 75-cm2 flasks (Corning Glass). The astrocyte monolayers were >98% pure as determined by GFAP immunoreactivity. Confluent astrocyte monolayers were changed to Dulbecco's modified Eagle's media devoid of serum prior to treatment. Stock solutions (20 mm) of ferric ammonium citrate (FAC) (Sigma), and 1,10-phenanthroline (Phen) (Sigma) were prepared in distilled water and directly applied to the monolayer at the indicated final concentrations. Each flask was treated with either of the following: (a) vehicle (water) as control group; (b) Phen at 100 μm during 48 h followed by 24 h at 50 μm;(c) FAC 50 μm during 4 days; (d) FAC treatment as in c followed by Phen treatment as in b in the absence of iron. Characterization of Detergent-insoluble MT-FTL Ferritin from Astrocyte Cultures—Cerebral cortical astrocytes cultures were homogenized in lysis buffer (3 ml of 50 mm Tris-HCl (pH 7.4), 1% SDS, 30 units/ml benzonase, 2 mm MgCl2) containing Complete protease inhibitor mixture (Roche Applied Science) and incubated for 15 min at room temperature. Lysates containing equal amounts of protein were ultracentrifuged at 46,000 rpm (TLA 110, Beckman) for 25 min at 4 °C. The supernatant (SDS-soluble) was removed, and the SDS-insoluble pellet was resuspended in lysis buffer and then subjected to another step of centrifugation in the same conditions. The final pellet was resuspended in 5× Laemmli sample buffer and heated for 10 min at 95 °C. The SDS-soluble, -insoluble, and total cell lysates (before SDS extraction) were resolved on 4–20% gradient SDS-PAGE (Pierce) and transferred to nitrocellulose membranes (Amersham Biosciences). Membranes were blocked for1 h in 70 mm Tris-buffered saline, 0.1% Tween 20, and 5% nonfat dry milk, followed by an overnight incubation with polyclonal antibodies (1283) against the MT-FTL polypeptide, as described previously (9 (link), 29 (link)) at 1:10,000. After washing, membranes were incubated with peroxidase-conjugated secondary antibody (GE Healthcare) for 1 h, washed, and developed using the ECL chemiluminescent detection system (GE Healthcare). MT-FTL recombinant polypeptides were loaded and used as positive control.
Sequence comparison between WT- and MT-FTL polypeptide. The wild type FTL polypeptide (WT-FTL) consists of 175 amino acids. The p.Phe167SerfsX26 mutant polypeptide (MT-FTL) has 191 amino acids and a different C-terminal sequence (underlined). The boxes indicate the five α-helical domains in the WT-FTL polypeptide according to Protein Data Bank accession number 2FG4. The mutant C-terminal sequence contains both metal-binding and hydrophobic groups.
MT-FTL polypeptides assemble into 24-mer homopolymers.A, elution profiles of purified WT- and MT-FTL apoferritin homopolymers from a Superose 6 column at pH 7.4 in 0.05 m Tris, 0.15 m NaCl. Retention times for both proteins are shown. Arrows indicate the elution time for the molecular weight markers. B, ultrastructural characterization of WT- and MT-FTL homopolymers by TEM. The dark cores most likely represent Nanovan that has penetrated in some cases the interior of the 24-mers. Bars, 10 nm. C, native PAGE (3–8% (pH7.4)) of 0.5 μm WT- and MT-FTL proteins loaded before the removal of iron and stained with Coomassie Blue (protein staining) and with Prussian blue (iron staining).
Immunofluorescence of Cultured Cells—Astrocyte cultures in Lab-Tek chambered coverglass slides (Nunc) were fixed for 15 min with 4% paraformaldehyde in PBS at 4 °C. Briefly, the slides were washed successively with PBS, permeabilized with 0.1% Triton X-100 for 15 min, and incubated for 1 h at room temperature in blocking solution (0.1% Triton X-100, 2% bovine serum albumin in PBS). The cultures were incubated overnight at 4 °C with the primary antibodies diluted in blocking solution, washed with PBS, and further incubated for 1 h at room temperature with the secondary antibodies diluted in blocking solution. The slides were then washed with PBS, rinsed with distilled water, and mounted with the Prolong Gold antifade mounting reagent (Molecular Probes). Primary antibodies used were monoclonal antibody to GFAP (1:400; Sigma) and polyclonal antibody against MT-FTL (1283). Secondary antibodies used were Alexa 488 Fluor-conjugated goat anti-rabbit and Alexa Fluor 594-conjugated goat anti-mouse (4 μg/ml; Molecular Probes). Images were captured with a Zeiss LSM-510 confocal scanner attached to a Zeiss Axiovert 100 M inverted microscope.
Baraibar M.A., Barbeito A.G., Muhoberac B.B, & Vidal R. (2008). Iron-mediated Aggregation and a Localized Structural Change Characterize Ferritin from a Mutant Light Chain Polypeptide That Causes Neurodegeneration. The Journal of Biological Chemistry, 283(46), 31679-31689.
The H2O2 assay was determined using the eFOX reagent (Cheeseman et al. 2006 (link)). The modified ferrous ammonium sulfate/xylenol orange (FOX) assay was preferred because of its sensitivity, stability, and adaptability to a large number of samples. Homogenization was performed using ice-cold acetone containing 25 mM H2SO4. Then samples were centrifuged for 5 min at 3000 × g at 4 °C. For 50 μl of the supernatant, 950 μl (250 μM ferrous ammonium sulfate, 100 μM sorbitol, 100 μM xylenol orange, 1% ethanol, v/v) of eFOX reagent was used. The reaction mixtures were incubated at room temperature for 30 min and absorbance at 550 and 800 nm was determined. H2O2 concentrations were calculated via a standard curve prepared with known concentrations of H2O2.
Gokce A., Sekmen Cetinel A.H, & Turkan I. (2024). Involvement of GLR-mediated nitric oxide effects on ROS metabolism in Arabidopsis plants under salt stress. Journal of Plant Research, 137(3), 485-503.
Based on liquid fermentation medium, 3% glucose, sucrose, maltose, fructose, and xylose were selected as carbon sources. Totals of 0.5% peptone, yeast extract, ammonium sulfate, ammonium chloride, and sodium nitrate were selected as nitrogen sources. Dipotassium hydrogen phosphate, ferrous sulfate heptahydrate, copper sulfate pentahydrate, sodium chloride, and ammonium chloride were used as inorganic salts, the concentration was 0.05%, and the other ingredients were the same as those in the liquid fermentation medium. The cultures were incubated at 18 • C and 150 rpm for 132 h, with three biological replicates per treatment. The extracellular polysaccharide content was determined by the phenol-sulfuric acid method.
Li X., Sun Q., Li S., Chen W., Shi Z., Xu Z., Xu L., Chen M., & Li Z. (2024). Production with Fermentation Culture and Antioxidant Activity of Polysaccharides from Morchella esculenta. Fermentation, 10(1), 46-46.
Ramos-Guivar J.A., Alca-Ramos Y.V., Manrique-Castillo E.V., Mendoza-Villa F., Checca-Huaman N.R., Rueda-Vellasmin R, & Passamani E.C. (2024). Pyroclastic Dust from Arequipa-Peru Decorated with Iron Oxide Nanoparticles and Their Ecotoxicological Properties in Water Flea D. magna. Nanomaterials, 14(9), 785.
Ferrous ammonium sulfate is a chemical compound commonly used in laboratory settings. It is a crystalline solid that serves as a source of ferrous ions. The compound's core function is to provide a stable and readily available form of iron for various analytical and experimental procedures.
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Ferrous sulfate is a chemical compound that consists of iron(II) and sulfate ions. It is a green crystalline solid that is commonly used as a dietary supplement and in various industrial applications.
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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
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Ferrous sulfate heptahydrate is an inorganic compound with the chemical formula FeSO4·7H2O. It is a green crystalline solid that is commonly used as a source of iron in various applications.
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Sulfuric acid is a highly corrosive, colorless, and dense liquid chemical compound. It is widely used in various industrial processes and laboratory settings due to its strong oxidizing properties and ability to act as a dehydrating agent.
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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.
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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
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Ammonium hydroxide is an aqueous solution of ammonia. It is a clear, colorless liquid with a pungent odor. Ammonium hydroxide is commonly used as a pH adjustor, a cleaning agent, and a reagent in various laboratory applications.
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Ascorbic acid is a chemical compound commonly known as Vitamin C. It is a water-soluble vitamin that plays a role in various physiological processes. As a laboratory product, ascorbic acid is used as a reducing agent, antioxidant, and pH regulator in various applications.
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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.
Ammonium ferrous sulfate is used in a variety of applications, including as a fertilizer, an oxidizing agent, and a reducing agent. It is also commonly used in the treatment of iron deficiency anemia, as it is a source of ferrous iron that can be absorbed by the body.
Compared to other iron supplements, ammonium ferrous sulfate is unique in that it contains both ammonium and ferrous ions. This combination can make it more readily absorbed by the body, making it an effective treatment for iron deficiency. However, it's important to note that individual responses may vary, and it's always best to consult with a healthcare professional before starting any new iron supplement regimen.
One potential challenge with ammonium ferrous sulfate is that it can cause gastrointestinal side effects, such as nausea, constipation, or diarrhea, in some individuals. Additionally, it's important to properly store and handle ammonium ferrous sulfate, as it can be reactive and potentially hazardous if not used correctly.
PubComepare.ai can be a valuable tool for researchers working with ammonium ferrous sulfate. The platform's AI-driven analysis can help you more efficiently screen protocol literature, identify critical insights, and pinpoint the most effective protocols related to ammonium ferrous sulfate for your specific research goals. This can enable you to choose the best options for reproducibility and accuracy, streamlining your workflow and helping you achieve better results.
More about "Ammonium ferrous sulfate"
Ammonium ferrous sulfate, also known as ferrous ammonium sulfate or ferrous sulfate ammonium, is a versatile inorganic compound with the chemical formula (NH4)2Fe(SO4)2.
This crystalline salt is widely used in various applications, including as a fertilizer, oxidizing agent, and reducing agent.
The compound is composed of ammonium (NH4+), ferrous (Fe2+), and sulfate (SO4(2-)) ions, giving it a distinctive green or violet color.
Ammonium ferrous sulfate is soluble in water, making it easily accessible for research and practical uses.
One of the key applications of ammonium ferrous sulfate is in the treatment of iron deficiency anemia.
The ferrous ions in the compound can be absorbed by the body to help replenish iron levels and alleviate the symptoms of anemia.
Researchers may use ammonium ferrous sulfate in their studies to investigate its medicinal properties and potential therapeutic uses.
Beyond its medicinal applications, ammonium ferrous sulfate finds use as an oxidizing agent, reducing agent, and in the production of various other chemical compounds.
Reserchers may utilize this versatile substance to explore its chemical properties, reactivity, and potential industrial applications.
When conducting research with ammonium ferrous sulfate, it's important to consider related compounds such as ferrous sulfate, ferrous sulfate heptahydrate, and hydrochloric acid, which may be used in conjunction or as precursors.
Additionally, substances like sulfuric acid, sodium hydroxide, methanol, ammonium hydroxide, and ascorbic acid may be relevant in the context of ammonium ferrous sulfate research and applications.
By understanding the comprehensive landscape of ammonium ferrous sulfate and its related compounds, researchers can optimize their workflows, identify the best protocols and products, and ultimately achieve more effective and efficient results in their studies.
