PubMed · 4701512
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A L Linch, E R Hendrickson, M Katz, J R Martin, G O Nelson, J N Pattison, A L Vander Kolk, R B Weidner. 1973. Liquid chromatography.. https://pubmed.ncbi.nlm.nih.gov/4701512/
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The contamination of water resources by uranyl (UO22+) ions poses significant environmental and health risks, requiring the development of efficient and sustainable remediation strategies. Adsorption-based techniques have emerged as promising approaches in the field of UO22+ removal, but the design of cost-effective, high-capacity, and environmentally friendly adsorbents remains challenging. In this study, a three-dimensional porous nano-hydroxyapatite@gelatin (nHAP@Ge) composite was synthesized through glutaraldehyde cross-linking, combining the structural stability of Ge with the high uranium affinity of nHAP. The optimized nHAP@Ge, with a nHAP:Ge mass ratio of 1:0.5, exhibited exceptional UO22+ removal efficiency (97 %), along with high adsorption capacity (364.03 mg/g). Systematic characterizations using scanning electron microscopy (SEM), thermogravimetric analysis (TGA), Fourier transform infrared (FT-IR) spectroscopy, and X-ray photoelectron spectroscopy (XPS) methods revealed that the porous structure and surface functional groups (-OH, Ca2+, and PO43-) of the material synergistically contributed to binding UO22+ species. Furthermore, the incorporation of nHAP into the Ge framework resulted in enhanced thermal stability while significantly improving the UO22+ adsorption performance. This work presents a scalable, eco-friendly, and recyclable strategy for the effective treatment of uranium-contaminated water, with potential applications in nuclear wastewater treatment and environmental remediation.
alpha s1- and beta-Caseins have a sequence cluster -Ser(P)-Ser(P)-Ser(P)-Glu-Glu- which is not present in kappa-casein and the whey PP3 component. The affinity of these phosphoproteins for the iron(III)-iminodiacetic acid (IDA) complex immobilized on Sepharose was studied as a function of pH, urea concentration, calcium ion concentration, enzymatic dephosphorylation and temperature. The affinity of the three polyphosphorylated proteins (alpha s1- and beta-caseins, PP3) was similar. The sequence cluster was not a specific recognition pattern of the iron(III) ion. These three proteins presented a site of high affinity and a site of weak affinity. kappa-Casein, which had only one Ser(P) residue, presented only the site of weak affinity. Their primary site which was absent after dephosphorylation or calcium ion addition required the presence of at least two Ser(P) residues close in space. Their secondary site was sensitive to the presence of urea. It was sensitive to pH variation for PP3 and kappa-casein. The study of the affinity of a few free amino acids towards iron(III)-IDA showed that the secondary site involved tryptophan and tyrosine residues for alpha s1- and beta-caseins, histidine residues for PP3 and cysteine residues for kappa-casein.
Comb-like polyethylene oxide (PEO) surfaces were prepared on low-density polyethylene (PE). The comb-like PEO chain density was changed gradually along the sample lengths by corona discharge treatment with gradually increasing power and the following graft copolymerization of poly(ethylene glycol) monomethacrylate macromers (PEO-MA). The macromers with different PEO repeat unit, 1, 5, and 10, were used. The prepared comb-like PEO gradient surfaces were characterized by water contact angle, Fourier transform infrared spectroscopy in the attenuated total reflectance mode, and electron spectroscopy for chemical analysis. All these measurements indicated that the PEO chains are grafted on the PE surface with gradually increasing density of PEO. Plasma protein adsorption and platelet adhesion on the PEO gradient surfaces decreased with increasing PEO chain length and surface density. As observed by scanning electron microscopy, PEO10-MA-grafted surface with high PEO density was very effective in preventing protein adsorption and platelet adhesion and did not activate the platelets.