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Publications (5)12.48 Total impact

  • Jie Tan, Wei Zhang, Yao-Hui Lv, Ai-Lin Xia
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    ABSTRACT: Mn-CeO2 submicrorods have been obtained from anomalous CeO2 particles though a novel composite-hydroxide-salt-mediated (CHSM) approach. This method is based on a reaction between a metallic salt and a metallic oxide in a solution of composite-hydroxide-salt eutectic at ~225 ºC and normal atmosphere without using an organic dispersant or capping agent. The magnetic measurement of the Mn-CeO2 submicrorods exhibits an enhanced ferromagnetic property at room temperature with a remanence magnetization (Mr) of 1.4 × 10-3 emu.g-1 and coercivity (Hc) of 75 Oe. The UV-visible spectra reveal that the absorption peak of the CeO2 shifts from ultraviolet region to visible light region after being doped with Mn ions. The room temperature ferromagnetic properties and light absorption of the Mn-CeO2 submicrorods would have wide applications in spintroics and photocatalysis field.
    Materials Research 08/2013; 16(4):689-694. · 0.52 Impact Factor
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    Yao-Hui Lv, Wei Zhang, Hong Liu
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    ABSTRACT: In the crystal structure of the title salt, C(5)H(6)N(3)O(2) (+)·C(6)H(5)O(4)S(-), N-H⋯O and O-H⋯O hydrogen bonds link the cations and anions. The dihedral angle between the rings of the cation and anion is 79.91 (6)°.
    Acta Crystallographica Section E Structure Reports Online 07/2012; 68(Pt 7):o2169. · 0.35 Impact Factor
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    ABSTRACT: Deseasin MCP-01 is a bacterial collagenolytic serine protease. Its catalytic domain alone can degrade collagen, and its C-terminal PKD domain is a collagen-binding domain (CBD) that can improve the collagenolytic efficiency of the catalytic domain by an unknown mechanism. Here, scanning electron microscopy (SEM), atomic force microscopy (AFM), zeta potential, and circular dichroism spectroscopy were used to clarify the functional mechanism of the PKD domain in MCP-01 collagenolysis. The PKD domain observably swelled insoluble collagen. Its collagen-swelling ability and its improvement to the collagenolysis of the catalytic domain are both temperature-dependent. SEM observation showed the PKD domain swelled collagen fascicles with an increase of their diameter from 5.3 μm to 8.8 μm after 1 h of treatment, and the fibrils forming the fascicles were dispersed. AFM observation directly showed that the PKD domain bound collagen, swelled the microfibrils, and exposed the monomers. The PKD mutant W36A neither bound collagen nor disturbed its structure. Zeta potential results demonstrated that PKD treatment increased the net positive charges of the collagen surface. PKD treatment caused no change in the content or the thermostability of the collagen triple helix. Furthermore, the PKD-treated collagen could not be degraded by gelatinase. Therefore, though the triple helix monomers were exposed, the PKD domain could not unwind the collagen triple helix. Our study reveals the functional mechanism of the PKD domain of the collagenolytic serine protease MCP-01 in collagen degradation, which is distinct from that of the CBDs of mammalian matrix metalloproteases.
    Journal of Biological Chemistry 05/2010; 285(19):14285-14291. · 4.65 Impact Factor
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    ABSTRACT: Deseasin MCP-01 is a bacterial collagenolytic serine protease. Its catalytic domain alone can degrade collagen, and its C-terminal PKD domain is a collagen-binding domain (CBD) that can improve the collagenolytic efficiency of the catalytic domain by an unknown mechanism. Here, scanning electron microscopy (SEM), atomic force microscopy (AFM), zeta potential, and circular dichroism spectroscopy were used to clarify the functional mechanism of the PKD domain in MCP-01 collagenolysis. The PKD domain observably swelled insoluble collagen. Its collagen-swelling ability and its improvement to the collagenolysis of the catalytic domain are both temperature-dependent. SEM observation showed the PKD domain swelled collagen fascicles with an increase of their diameter from 5.3 mum to 8.8 mum after 1 h of treatment, and the fibrils forming the fascicles were dispersed. AFM observation directly showed that the PKD domain bound collagen, swelled the microfibrils, and exposed the monomers. The PKD mutant W36A neither bound collagen nor disturbed its structure. Zeta potential results demonstrated that PKD treatment increased the net positive charges of the collagen surface. PKD treatment caused no change in the content or the thermostability of the collagen triple helix. Furthermore, the PKD-treated collagen could not be degraded by gelatinase. Therefore, though the triple helix monomers were exposed, the PKD domain could not unwind the collagen triple helix. Our study reveals the functional mechanism of the PKD domain of the collagenolytic serine protease MCP-01 in collagen degradation, which is distinct from that of the CBDs of mammalian matrix metalloproteases.
    Journal of Biological Chemistry 03/2010; 285(19):14285-91. · 4.65 Impact Factor
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    ABSTRACT: The electrokinetic properties of Nd:YAG nanopowder with particles of about 40nm in diameter were investigated by measuring the zeta potential of a stable YAG (Y3Al5O12) aqueous slurry. Ammonium poly(acrylic acid) polyelectrolyte was used as dispersant to adjust the electrokinetic properties of the Nd:YAG slurry. The effect of the pH of the slurry and of the polyelectrolyte concentration on the stability of the suspension are discussed in this study. The optimal pH value and the amount of dispersant needed to obtain a stable Nd:YAG nanoparticle slurry were determined. Highly consistent Nd:YAG nanoparticle slurries with optimal pH and dispersant concentration were prepared by ball milling. The rheological behavior of Nd:YAG slip with different solid loading (60–70wt%) has been studied by measuring the viscosity and shear stress as a function of shear rate. Slip with solid loadings of 65wt% shows near-Newtonian behavior but becomes non-Newtonian with typical shear-thinning behavior above this solid loading value. The density and microstructure of the cast product bears a direct relationship to the state of the slip induced by alternation of the pH and the concentration of the dispersant as well as the solid loading.
    Journal of Materials Science 01/2010; 45(3):706-712. · 2.31 Impact Factor