sodium-dodecyl-sulfate and 2-4-dinitrophenylhydrazine

2,4-Dinitrophenylhydrazine immobilized on sodium dodecyl sulfate (SDS)-coated magnetite and was used for removal of Cd(II) and Ni(II) ions from aqueous solution. The prepared product was characterized by X-ray diffraction (XRD) analysis, Fourier transform infrared spectroscopy (FT-IR), and scanning electron microscopy (SEM). The size of the nanoparticles according to SEM was obtained around 20-35 nm. In batch tests, the effects of pH, contact time, initial metal concentration, and temperature were studied. The kinetic and equilibrium data were modeled with recently developed models. The adsorption kinetics and isotherms were well fitted by the fractal-like pseudo-second-order model and Langmuir-Freundlich model, respectively. Maximum adsorption capacity by this adsorbent is 255.1 mg g(-1) for Cd(II) ion and 319.6 mg g(-1) for Ni(II) ion at pH 7.0 and 25 °C. The method was successfully applied to the removal of metal cations in real samples (tap water, river water, and petrochemical wastewater).

Topics: Adsorption; Cadmium; Drinking Water; Hydrogen-Ion Concentration; Kinetics; Magnetite Nanoparticles; Microscopy, Electron, Scanning; Nickel; Phenylhydrazines; Rivers; Sodium Dodecyl Sulfate; Spectroscopy, Fourier Transform Infrared; Temperature; Wastewater; Water Pollutants, Chemical; Water Purification; X-Ray Diffraction

It has been demonstrated that an age-associated increase in protein oxidation is a highly selective rather than random phenomenon. Addition of carbonyl groups is a widely used marker for the detection of oxidative damage to the proteins. Carbonyls can be detected immunochemically using antibodies against dinitrophenylhydrazine (DNPH), a reagent that specifically reacts with protein carbonyl groups. In this paper, a procedure for the identification of oxidized proteins during aging or under pathological conditions is described. Protein samples were treated with DNPH and then separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by immunochemical detection. Proteins exhibiting positive immunostain were then purified by SDS-PAGE followed by isoelectric focusing. The focused protein band was further concentrated by another run of SDS-PAGE and transferred onto Immobilon-P membrane. The identity of the protein was revealed by automated Edman microsequencing and a computer database search. This method is successfully demonstrated for the identification of housefly arginine kinase, a cytosolic protein that is involved in the energy metabolism of insect muscle cells.

Topics: Amino Acid Sequence; Animals; Electrophoresis, Polyacrylamide Gel; Immunochemistry; Isoelectric Focusing; Membranes, Artificial; Molecular Sequence Data; Muscle Proteins; Oxidation-Reduction; Phenylhydrazines; Proteins; Sequence Analysis; Sodium Dodecyl Sulfate; Staining and Labeling