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  • Author or Editor: S.E. Chen x
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Lipopolysaccharide and b-1,3-glucan binding protein (LGBP) is a pattern recognition receptor that can recognize and bind LPS and b-1,3-glucan. LGBP has crucial roles in innate immune defense against Gram-negative bacteria and fungi. In this study, LGBP functions in Portunus trituberculatus innate immunity were analyzed. First, the mRNA expression of PtLGBP in hemocytes, hepatopancreas, and muscle toward three typical pathogen-associated molecular patterns (PAMPs) stimulations were examined using real-time PCR. Results show that the overall trend of relative expressions of the LGBP gene in three tissues is consistent, showing up-down trend. In each group, the highest expression of the LGBP gene was at 3 and 12 h post-injection. The LGBP gene is also expressed significantly higher in the hemocytes and hepatopancreas than in the muscle. The highest level of LGBP was in the lipopolysaccharides (LPS) and glucan-injected group, whereas the lowest level was in the PGN-injected group. Furthermore, bacterial agglutination assay with polyclonal antibody specifically for PtLGBP proved that the recombinant PtLGBP (designated as rPtLGBP) could exhibit obvious agglutination activity toward Gram-negative bacteria Escherichia coli, Vibrio parahaemolyticus, and V. alginolyticus; Gram-positive bacteria Bacillus subtilis; and fungi Saccharomyces cerevisiae. LGBP in Portunus trituberculatus possibly served as a multi-functional PRR. In addition, LGBP is not only involved in the immune response against Gram-negative and fungi, as manifested in other invertebrates, but also has a significant role in anti-Gram-positive bacteria infection.

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This study optimised the hydrolysis process of chicken plasma protein and explored the in vivo antioxidant activity of its hydrolysates. The results showed that alkaline protease provided the highest degree of hydrolysis (19.30%), the best antioxidant effect in vitro. The optimal hydrolysis process of alkaline protease was: temperature 50 °C, time 8 h, [E]/[S] 7000 U g−1, pH 7.5. Antioxidant studies in vivo showed that the low, medium, and high dose groups significantly reduced the serum MDA and protein carbonyl content (P < 0.05) and significantly increased the serum SOD and GSH contents (P < 0.05). The results of HE staining of the liver showed that the liver cells in the model group were severely damaged, but the chicken plasma protein hydrolysates could alleviate this pathological damage. Chicken plasma protein hydrolysis products had certain antioxidant activity.

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Distribution coefficients of technetium and ruthenium are determined under different conditions with CCl4, cyclohexanone, and 5% tri-isooctylamine (TIOA)/xylene. A method for analyzing99Tc in environmental samples has been developed by solvent extraction in which the valences of technetium and ruthenium are controlled with H2O2 and NaClO. Technetium and ruthenium which are oxidized to TcO 4 and RuO 4 by NaClO are separated by extraction with CCl4 at pH 4. The RuO 4 is reduced to low valence and technetium is kept in the TcO 4 state with H2O2. Technetium, ruthenium, and other nuclides are subsequently separated by solvent extraction with cyclohexanone and 5% TIOA/xylene. The decontamination of the procedure is 1.35·105 for103Ru and 1.66·105 for110mAg. The chemical yield of technetium-99 is 55%.

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Inhalation is one of the most important routes for aerosol particles of uranium compounds to enter the body. The main step for uranium to be available for blood circulation and for interaction with bio-molecules is the dissolution of the particles. Particle size effects on dissolution of uranium dioxide and uranium ore were studied in simulated lung fluid using the “batch/filter” method. Samples were fractionated to ten size ranges from <0.43 μm to >10 μm by cascade impaction prior to dissolution experiments. Dependence of dissolution kinetics on particle size and on the amount of uranium trioxide contained in the particles was observed.

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