Hyperuricemia is an independent risk factor for renal function decline. Patients treated with ULT who achieved sUA < 6 mg/dl on ULT showed a 37% reduction in outcome events.

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In this paper, Mn doped BiFeO₃ were firstly synthesized by hydrothermal process. The influence of Mn doping on structural, optical and magnetic properties of BiFeO₃ was studied. The different amounts of Mn doping in BiFeO₃ were characterized by X-ray diffraction, Scanning Electron Microscope, Energy Dispersive X-ray Spectroscope, UV-Vis diffuse reflectance spectroscopy and magnetic measurements. The X-ray diffraction (XRD) patterns confirmed the formation of pure phase rhombohedral structure in BiFe(1−x) Mn (x) O₃ (x = 0.01, 0.03, 0.05, 0.07) samples. The morphologies and chemical compositions of as-prepared samples could be observed by Scanning Electron Microscope (SEM) and Energy Dispersive X-ray Spectroscope (EDS). A relative large saturated magnetization (Ms) of 0.53 emu/g for x = 0.07 sample was obtained at room temperature, which is considered to be Mn ions doping. UV-Vis diffuse reflectance spectroscopy showed strong absorption of light in the range of 200–1000 nm, indicating the optical band gap in the visible region for these samples. This implied that BiFe(1−x) Mn(x)O₃ may be a potential photocatalyst for utilizing solar energy.

In solutions of myofibrillar protein extracted from giant squid (Dosidicus 23 gigas), the size-coarsening process of protein nanofiber is complex. At high 24 temperature (25 o C), nanofiber keeps growth but with two distinguishable patterns, 25 slow rate at the initial stage with t 0.2 and the fast one at the late stage with t 2.3 . The 26 intersection of these two slopes is around 300 min. Meanwhile, protein concentration 27 in solution enhances as well. These behaviors contradict to the prediction of Ostwald 28 ripening. Thus, we call this process as abnormal. These abnormal behaviors come 29 from the conformation change of some types of constitution protein molecules with 30 chemical potential reduction when they dissolve from nanofiber to solution. On the 31 other hand, low temperature (10 o C) depresses this size growth. This observation 32 suggests that temperature regulates protein molecule conformation change in 33 nanofiber. The consequence of this abnormal Ostwald ripening process is that all 34 protein molecules in nanofiber are redistributed. Protein molecules with the absence 35 of conformation change in dissolution accumulate in nanofiber to cause it growing, 36 while the rest concentrates in solution. 37 Wilhelm Ostwald descried the phenomenon of large particle growth in 50 the cost of small one as Ostwald ripening due to the surface tension which is 51 proportional to the particles curvature(1-3). As a result, the solute concentration keeps 52 reduction throughout size-coarsening process. Meanwhile, an essential prerequisite, 53 no molecular conformation change when a molecule transfers from one phase to 54 another, exists but is always ignored. This condition is satisfied in inorganic and 55 organic compounds. However, in protein solutions containing particles with various 56 sizes, it should be cautious to apply Ostwald ripening theory in the size-coarsening 57 process because protein molecules are sensitive to the ambient conditions. Even salt 58 concentration variation could induce protein molecule conformation change(4). Thus, 59it is worth to verify Ostwald ripening theory in protein solutions. 60 The existence of nanofiber in solutions of myofibrillar protein extracted from 61 giant squid (Dosidicus gigas) is verified(5). In order to investigate its size-coarsening 62 process in this solution, 2.73 mg mL -1 myofibrillar protein was diluted 10 times by the 63 buffer solution, and was assessed by the dynamic light scattering (DLS) technique and 64 the fluorescence spectroscopy (FS) technique immediately. 65In Fig. 1a, the pattern of light intensity on time depends on the temperature. High 66 temperature (25 o C) allows the light intensity monotonically growing, while low 67 temperature (10 o C) depresses this growth with almost constant light intensity 68 throughout the experiment. Due to high activity of enzymolysis in myofibrillar protein 69at 25 o C(6), it is necessary to estimate its influence in this study. In Fig, 1b, the 70 apparent concentrations of myofibrillar protein in three...

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