Znso4 h2o

Manufactured by Merck Group

Sourced in Australia, United States

ZnSO4·H2O is a chemical compound that consists of zinc sulfate and water. It is a white, crystalline solid that is commonly used in various laboratory and industrial applications.

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8 protocols using znso4 h2o

Synthesis and Characterization of ZnLS and ZnEDTA Complexes

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The ZnLS complexes were formed by mixing a solution of ZnSO₄⋅ H₂O (Merck) and the suitable amount of LS to complex Zn, calculated based on their maximum complexing capacity (Table 1). In order to ensure that all the quantity of element is complexed, an amount of 10% LS was added in excess. Solutions were left to stand overnight, filtered through 0.45 μm Millipore membrane and made up to volume.
For the preparation of the ZnEDTA solution, Na₂EDTA (Merck) was dissolved in sufficient NaOH (1:3 molar ratio) and an amount of ZnSO₄⋅ H₂O (Merck) calculated to be 5% in excess of the molar amount of ligand was then slowly added. During the chelation process, pH was maintained between 6.0 and 8.0. The solution was left to stand overnight, filtered through 0.45 μm Millipore membrane and made up to volume.

Cieschi M.T., Benedicto A., Hernández-Apaolaza L, & Lucena J.J. (2016). EDTA Shuttle Effect vs. Lignosulfonate Direct Effect Providing Zn to Navy Bean Plants (Phaseolus vulgaris L ‘Negro Polo’) in a Calcareous Soil. Frontiers in Plant Science, 7, 1767.

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Heavy Metal Tolerance Assay

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Davis minimal medium (DMM), 4-aminoantipyrine, potassium ferrocyanide, catechol, sodium hydroxide pellets used in this study were purchased from HiMedia Laboratories Pvt. Ltd. Mumbai, phenol, 2-mercaptoethanol, ammonium hydroxide, glycerol, disodium EDTA, primers, acids and solvents were procured from Sigma, Aldrich, Tris Base, Agarose from Bio Basic Inc. All the following heavy metals CoCl₂.2H₂O, ZnSO₄.H₂O, (CH₃COO)₂Pb.3H₂O, HgCl₂, CdCl₂, CuSO₄.5H₂O, NiCl₂.6H₂O, MnCl₂.4H₂O, and K₂Cr₂O₇ were purchased from Merck Millipore, Taq DNA polymerase Master Mix from Ampliqon and PCR purification Kit from Favorgen Biotech Corp. were used.

Duraisamy P., Sekar J., Arunkumar A.D, & Ramalingam P.V. (2020). Kinetics of Phenol Biodegradation by Heavy Metal Tolerant Rhizobacteria Glutamicibacter nicotianae MSSRFPD35 From Distillery Effluent Contaminated Soils. Frontiers in Microbiology, 11, 1573.

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Biomass Conversion via Catalytic Pyrolysis

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Raw materials, including cellulose, D-allose (C₆H₁₂O₆), D-glucose (C₆H₁₂O₆), xylan, 5-HMF (C₆H₆O₃), LGA (C₆H₁₀O₅) and LGO (C₆H₆O₃), were reagent grade with a purity >99% and were purchased from Merck Co Ltd. The chemicals for catalyst synthesis, including Pd(NO₃)₂·2H₂O (~40% Pd basis), ZnSO₄·H₂O (≥99.9% trace metals basis) and ZnSO₄·7H₂O (ACS reagent, 99%), were also purchased from Merck Co Ltd. The two real biomass feedstocks, corncob and sugarcane bagasse with particle sizes of 150–250 μm, were sourced from Oz Gun Mart in New South Wales, Australia and Sugarcane Juice Bar in Melbourne, Australia, respectively. They were dried in an oven at 105 °C for 15 h prior to the pyrolysis experiments.

Zhou Q., Gu J., Wang J., De Girolamo A., Yang S, & Zhang L. (2023). High production of furfural by flash pyrolysis of C6 sugars and lignocellulose by Pd-PdO/ZnSO4 catalyst. Nature Communications, 14, 1563.

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Synthesis and Characterization of ZNF750 Peptides

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The 27-residue peptides Z* and Z*(C34A, H39A), corresponding to the fragment 25–51 of human ZNF750 (UniProt Q32MQ0), were synthesized by AAPPTec (Louisville, KY). Both peptides had their termini blocked by N-acetylation and C-amidation, were ≥90% pure by HPLC, and had molecular weights by mass spectrometry within 3 Daltons of those theoretically expected. ZnSO₄·H₂O (purity of ≥99.9%) was from Sigma (St. Louis, MO).

Rua A.J., Whitehead RD 3.r.d, & Alexandrescu A.T. (2023). NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750. Journal of Structural Biology: X, 8, 100093.

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Metal-Induced Amyloid Aggregation Assay

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A total of 0.1 M stock solutions of Cu(II) and Zn(II) (from CuSO₄.5(H₂O) and ZnSO₄(H₂O), respectively, purchased from Sigma (St. Louis, MO, USA)) were prepared in ultrapure water. Phosphate buffer was bought from Sigma-Aldrich (St. Louis, MO, USA) and dissolved in ultrapure water to reach a 0.1 M concentration. Bioluminescence grade HEPES buffer (sodium salt of 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid) was bought from Honeywell Fluka (Morristown, NJ, USA) and dissolved in ultrapure water to reach a 0.5 M concentration. Tris hydrochloride (Tris-HCl) was purchased from Fluka and dissolved in ultrapure water to reach 1 M concentration, and was adjusted with NaOH to pH 11.0. Guanidinium chloride >99% was bought from Alfa Aesar (Haverhill, MA, USA) and was freshly prepared by dissolving the powder in Tris-HCl 0.1 M to reach a 6 M concentration. A 5 mM ascorbate solution was freshly prepared a few minutes prior to each experimental set by dissolving sodium L-ascorbate (Sigma) in ultrapure water. Ethylene diamine tetraacetic acid (EDTA) was purchased from Sigma-Aldrich and dissolved in ultrapure water to reach a 40 mM concentration. A stock solution of Thioflavin T (ThT) at 250 μM was prepared in water without any further purification, with ThT bought from Acros Organics (Waltham, MA, USA).

Cheignon C., Collin F., Sabater L, & Hureau C. (2023). Oxidative Damages on the Alzheimer’s Related-Aβ Peptide Alters Its Ability to Assemble. Antioxidants, 12(2), 472.

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Preparation of Redox-Sensitive Fluorescent Probes

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Reagents were commercially available and were used as received.
Hepes buffer (sodium salt of 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid) was bought from Fluka (bioluminescence grade).
Phosphate buffer was prepared from K₂HPO₄ and KH₂PO₄ bought from Fluka.
The Cu(ii) and Zn(ii) sources were Zn(SO₄)(H₂O) and Cu(SO₄)(H₂O)₅ and purchased from Sigma.
A stock solution (5 mM) of ascorbate was prepared in Milli-Q water at room temperature just before beginning the experiment. Because ascorbate degrades quickly, a fresh solution was prepared each day.
A stock solution of coumarin-3-carboxylic acid (CCA, 5 mM) was prepared in phosphate buffer (500 mM, pH 7.1) at room temperature. The stock solution was stored at 4 °C.
A stock solution of Thioflavin T (ThT) at 250 μM was prepared in water without any further purification with ThT bought from Acros Organics.

Conte-Daban A., Day A., Faller P, & Hureau C. (2016). How Zn can impede Cu detoxification by chelating agents in Alzheimer's disease: a proof-of-concept study †Electronic supplementary information (ESI) available. See DOI: 10.1039/c6dt02308h Click here for additional data file.. Dalton Transactions (Cambridge, England : 2003), 45(39), 15671-15678.

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Pekin Duck Embryo and Duckling Tissue Study

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Twenty-day-old Pekin duck embryos and 1-day-old male Pekin ducks were purchased from Sichuan Mianying Duck Industry Co., Ltd. (Mianyang, China). ZnSO₄·H₂O, TPEN, LPS (Lipopolysaccharides from Escherichia coli O55:B5) and FITC-D (MW 3–5 kDa; Sigma, St. Louis, MO) were obtained from Sigma-Aldrich (Saint Louis, MO). TOR and β-actin were obtained from Thermo Fisher Scientific Co., Ltd. (Shanghai, China).

Xie Y., Wen M., Zhao H., Liu G., Chen X., Tian G., Cai J, & Jia G. (2021). Effect of zinc supplementation on growth performance, intestinal development, and intestinal barrier function in Pekin ducks with lipopolysaccharide challenge. Poultry Science, 100(12), 101462.

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Characterization of Zinc Finger Protein

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ZnSO₄•H₂O (purity ≥ 99.9%) was from Sigma (St. Louis, MO). 99.96% D₂O was from Cambridge Isotopes (Tewksbury, MA), and 4-nintophenyl acetate (4-NA) was from Sigma (St Louis, MO). The 27-residue Z7 peptide with the WT sequence, corresponding to the fragment 562–588 of human ZNF711 (UniProt Q9Y462), was custom synthesized at 96% HPLC purity by Biomatik (Kitchener, Canada). The Mut1 peptide was synthesized at 96% purity by AAPPTec (Louisville, KY) and Mut2 was made at 86% purity by Biomatik. All three peptides had their termini blocked by N-acetylation and C-amidation and had molecular weights by mass spectrometry within 1 Dalton of those theoretically expected from the sequence. Peptide concentrations were determined by absorption at 280 nm (A₂₈₀) using a molar extinction coefficient of 1,559 M⁻¹ cm⁻¹ for the unfolded Z7 in the absence of Zn²⁺. The peptide concentration to determine the extinction coefficient was determined with a BCA assay (Walker 2002 ). The value for the unfolded peptide is very close to that of 1,490 M⁻¹ cm⁻¹ predicted from its sequence with the ProtParam program (Gasteiger et al. 2005 ). For folded ZNF711 in the presence of Zn²⁺, we determined an A₂₈₀ extinction coefficient of 2,383 M⁻¹ cm⁻¹.

Rua A.J, & Alexandrescu A.T. (2024). Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure. bioRxiv.

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