PubMed · 6986697
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V M Nielsen. 1980-01-21. [Insulin administration].. https://pubmed.ncbi.nlm.nih.gov/6986697/
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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.
The adsorption of fibrinogen from a single protein solution and from binary mixtures of fibrinogen and high-molecular-weight kininogen (HK) to glass and four sulfonated polyurethane surfaces is reported. The effect of the single-chain (SCHK) and two-chain (TCHK) forms of HK on fibrinogen adsorption was investigated. Using radiolabeling methods, fibrinogen adsorption from a series of mixtures having the same weight ratio of fibrinogen to HK as in plasma (50:1), but varying in total concentration, was measured. Fibrinogen adsorption from the mixtures was reduced on all surfaces compared to the single-protein solution, confirming the highly surface-active nature of this protein. However, except for glass, there was no significant difference between the SCHK and TCHK forms. Polyacrylamide gel electrophoresis and immunoblotting analysis of the proteins eluted from the surfaces after contact with the fibrinogen-SCHK solutions indicated that although intact SCHK was essentially conserved, some transformation of SCHK to TCHK on the surface occurred during the course of the experiment. It is hypothesized that in purified form, in which HK is not complexed to prekallikrein or factor XI, the surface-binding domain is more available than in the complexed forms which are present in plasma. If so, then the removal of bradykinin by kallikrein, as occurs in generating TCHK, may not be required for the expression of surface-binding domain activity.
The validity of the conventional interpretation of IAsys biosensor profiles in terms of pseudo-first-order kinetic behavior is subjected to closer scrutiny by its application to simulated data for low- and high-affinity interactions between ligate and immobilized ligand. As might reasonably have been expected, analysis of the simulated data for the low-affinity system (association equilibrium constant of 10(5) M-1) in such terms returned the input association and dissociation rate constants (10(3) M-1 s-1 and 10(-2) s-1, respectively)-a consequence of essential compliance with the assumed constancy of ligate concentration in the liquid phase. For the high-affinity interaction (ka = 10(5) M-1 s-1, kd = 10(-2) s-1, KAX = 10(7) M-1) the ligate concentration was depleted by up to 35%, and hence its assumed constancy was clearly an untenable approximation. Whereas no symptomatic evidence of such violation (apart from the return of incorrect estimates of ka and kd) was evident from pseudo-first-order kinetic analysis of the adsorption profiles, the corresponding analysis of desorption profiles was more informative in that the data deviated demonstrably from pseudo-first-order kinetic behavior. A second-order kinetic analysis was therefore developed and shown to be applicable to adsorption and desorption profiles, irrespective of the validity or otherwise of the pseudo-first-order kinetic approximation. Experimental results obtained for the interaction of histidine-rich glycoprotein with immobilized IgG were then used to illustrate various features of the pseudo-first-order and second-order kinetic analyses, and to determine from the second-order analysis an association equilibrium constant of 2 x 10(8) M-1, which is 20-fold greater than the value obtained by interpretation of the profiles in terms of pseudo-first-order kinetic behavior.