SO4- and OH participated in the reaction together and OH played the main role in activating PS to AO7 decolorization based on the radical scavengers experiment. All of results indicate using biochar to activate PS for degradation of AO7 contaminated water is a promising method. BACKGROUND The optimal duration of filgrastim as primary febrile neutropenia (FN) prophylaxis in early breast cancer (EBC) patients is unknown, with 5, 7 or 10 days being commonly prescribed. This trial evaluates whether 5 days of filgrastim was non-inferior to 7/10 days. PATIENTS AND METHODS In this randomised, open-label trial, EBC patients who were to receive filgrastim as primary FN prophylaxis were randomly allocated to 5 vs 7 vs 10 days of filgrastim for all chemotherapy cycles. A protocol amendment in November 2017 allowed subsequent patients (N=324) to be randomised to either 5 or 7/10 days. The primary outcome was a composite of either FN or treatment-related hospitalisations. Secondary outcomes included chemotherapy dose reductions, delays, and discontinuations. Analyses were performed by per protocol (primary) and intention-to-treat and the non-inferiority margin was set at 3% for the risk of having FN and/or hospitalisation per cycle of chemotherapy. RESULTS Patient (N=466) were randomized to receive 5 (184, 39.5%), or 7/10 (282, 60.5%) days of filgrastim. In our primary analysis, the difference in risk of either FN or treatment-related hospitalisation per cycle was -1.52% (95%CI -3.22% to 0.19%) suggesting non-inferiority of a 5-day filgrastim schedule compared to 7/10-days. The difference in events per cycle for FN was 0.11% (95%CI -1.05 to 1.27) while for treatment-related hospitalisations it was -1.68% (95%CI -2.73% to -0.63%). The overall proportions of patients having at least one occurrence of either FN or treatment-related hospitalization were 11.8% and 14.96% for the 5- and 7/10-day groups respectively (Risk Difference -3.17%, 95%CI -9.51% to 3.18%). CONCLUSION Five days of filgrastim was non-inferior to 7/10 days. Given the cost and toxicity of this agent, 5 days should be considered standard of care. Surfactant Protein D (SP-D) is a collectin protein that participates in the innate immune defense of the lungs. SP-D mediates the clearance of invading microorganisms by opsonization, aggregation or direct killing, which are lately removed by macrophages. SP-D is found as a mixture of trimers, hexamers, dodecamers and higher order oligomers, "fuzzy balls". However, it is unknown whether there are differences between these oligomeric forms in functions, activity or potency. In the present work, we have obtained fractions enriched in trimers, hexamers and fuzzy balls of full-length recombinant human (rh) SP-D by size exclusion chromatography, in a sufficient amount to perform functional assays. We have evaluated the differences in protein lectin-dependent activity relative to aggregation and binding to E. coli, one of the ligands of SP-D in vivo. Fuzzy balls are the most active oligomeric form in terms of binding and aggregation of bacteria, achieving 2-fold binding higher than hexamers and 50% bacteria aggregation at very short times. Hexamers, recently described as a defined oligomeric form of the protein, have never been isolated or tested in terms of protein activity. rhSP-D hexamers efficiently bind and aggregate bacteria, achieving 50-60% aggregation at final time point and high protein concentrations. Nevertheless, trimers are not able to aggregate bacteria, although they bind to them. Therefore, SP-D potency, in functions that relay on the C-lectin activity of the protein, is proportional to the oligomeric state of the protein. The endo-β-1,4-mannanase from the hyperthermostable bacterium Thermotoga petrophila (TpMan) is an enzyme that catalyzes the hydrolysis of mannan and heteromannan polysaccharides. Of the three domains that comprise TpMan, the N-terminal GH5 catalytic domain and the C-terminal carbohydrate-binding domain are connected through a central ancillary domain of unknown structure and function. In this study, we report the partial crystal structure of the TpMan at 1.45 Å resolution, so far, the first modular hyperthermostable endo-β-1,4-mannanase structure determined. The structure exhibits two domains, a (β/α)8-barrel GH5 catalytic domain connected via a linker to the central domain with an immunoglobulin-like β-sandwich fold formed of seven β-strands. Functional analysis showed that whereas the immunoglobulin-like domain does not have the carbohydrate-binding function, it stacks on the GH5 catalytic domain acting as a thermostabilizing domain and allowing operation at hyperthermophilic conditions. The carbohydrate-binding domain is absent in the crystal structure most likely due to its high flexibility around the immunoglobulin-like domain which may act also as a pivot. These results represent new structural and functional information useful on biotechnological applications for biofuel and food industries. Long-chain (C20-24) polyunsaturated fatty acids (LC-PUFA) are physiologically important nutrients for vertebrates including fish. Previous studies have addressed the metabolism of LC-PUFA in the Amazonian teleost tambaqui (Colossoma macropomum), an emerging species in Brazilian aquaculture, showing that all the desaturase and elongase activities required to convert C18 polyunsaturated fatty acids (PUFA) into LC-PUFA are present in tambaqui. Yet, elongation of very long-chain fatty acid 4 (Elovl4) proteins, which participate in the biosynthesis of very long-chain (>C24) saturated fatty acids (VLC-SFA) and very long-chain polyunsaturated fatty acids (VLC-PUFA), had not been characterized in this species.  https://www.selleckchem.com/products/mivebresib-abbv-075.html  Here, we investigate the repertoire and function of two Elovl4 in tambaqui. Furthermore, we present the first draft genome assembly from tambaqui, and demonstrated the usefulness of this resource in nutritional physiology studies by isolating one of the tambaqui elovl4 genes. Our results showed that, similarly to other teleost species, two elovl4 gene paralogs termed as elovl4a and elovl4b, are present in tambaqui. Tambaqui elovl4a and elovl4b have open reading frames (ORF) of 948 and 912 base pairs, encoding putative proteins of 315 and 303 amino acids, respectively. Functional characterization in yeast showed that both Elovl4 enzymes have activity toward all the PUFA substrates assayed (183n-3, 182n-6, 184n-3, 183n-6, 205n-3, 204n-6, 225n-3, 224n-6 and 226n-3), producing elongated products of up to C36. Moreover, both Elovl4 were able to elongate 225n-3 to 245n-3, a key elongation step required for the synthesis of docosahexaenoic acid via the Sprecher pathway.