Weavermedeiros8832
At 298 K, the maximum adsorption capacity of As(III) is 20.16 mg/g. Regeneration studies find that CAFBs can be effectively regenerated by aeration into the NaOH solution. This study was to assess the anti-inflammatory potential of exopolysaccharide (EPS) produced by a medicinal fungus Cordyceps sinensis Cs-HK1. The EPS was isolated from the Cs-HK1 mycelial fermentation broth by ethanol precipitation and purified by deproteinization and dialysis. The EPS had a total sugar content of 74.8% and a maximum average molecular weight (MW) over 107 Da, and consisted mainly of glucose and mannose, and a small amount of galactose and ribose. In THP-1 and RAW264.7 cell cultures, EPS significantly inhibited lipopolysaccharide (LPS)-induced inflammatory responses of the cells including the release of NF-κB and several pro-inflammatory factors such as NO, TNF-α and IL-1β. In the murine model of LPS-induced acute intestinal injury, the oral administration of EPS to the animals effectively suppressed the expression of major inflammatory cytokines TNF-α, IL-1β, IL-10 and iNOS and alleviated the intestinal injury. The results suggest that the Cs-HK1 EPS has notable anti-inflammatory activity and can be a potential candidate for further development of new anti-septic therapeutics. To the best of our knowledge, this is the first report on the anti-inflammation of an EPS from C. sinensis fungal fermentation. The main systemic alterations present in bothropic envenomation are hemostasis disorders, for which the conventional treatment is based on animal-produced antiophidic sera. We have developed a neutralizing antibody against Bothrops pauloensis (B. pauloensis) venom, which is member of the genus most predominant in snakebite accidents in Brazil. Subsequently, we expressed this antibody in plants to evaluate its enzymatic and biological activities. The ability of single-chain variable fragment (scFv) molecules to inhibit fibrinogenolytic, azocaseinolytic, coagulant and hemorrhagic actions of snake venom metalloproteinases (SVMPs) contained in B. pauloensis venom was verified through proteolytic assays. The antibody neutralized the toxic effects of envenomation, particularly those related to systemic processes, by interacting with one of the predominant classes of metalloproteinases. This novel molecule is a potential tool with great antivenom potential and provides a biotechnological antidote to snake venom due to its broad neutralizing activity. This study presented the first purification and characterization of a hepatoprotective polysaccharide (PNPS-0.5 M) from the residue of Panax notoginseng (Burk.) F.H. Chen. This polysaccharide included a backbone of (4 → 1)-linked GalA and branches of (1→)-linked Araf, (1→)-linked Rhap, and (5 → 1)-linked Araf and had an extremely high molecular weight (2600 kDa). We investigated the hepatoprotective effects of PNPS-0.5 M on mice with alcoholic liver damage (ALD). After administration of PNPS-0.5 M, the levels of alanine aminotransferase (ALT), aspartate aminotransferase (AST), triglyceride (TG), and hepatic malondialdehyde (MDA) were reduced to normal. In contrast, hepatic levels of alcohol dehydrogenase (ADH) and the antioxidant enzymes superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) were elevated to normal. Further investigations indicated that PNPS-0.5 M activated Nrf2 signaling as a protective mechanism against Cyp2e1 toxicity in ALD mice. Meanwhile, it strengthened the ADH pathway and suppressed the CAT pathway of alcohol metabolism to prevent peroxide accumulation, thereby ameliorating ALD. In the present study, we describe a novel acidic polysaccharide from P. notoginseng with hepatoprotective activity that facilitates the development and utilization of P. notoginseng resources. V.Somatic cell nuclear transfer (SCNT) has potential applications in agriculture and biomedicine, but the efficiency of cloning is still low. In this study, the transcriptional profiles in cloned and fertilized embryos were measured and compared by RNA sequencing. Diphenyleneiodonium The 2-cell embryos were detected to identify the earliest transcriptional differences between embryos derived through IVF and SCNT. As a result, 364 genes showed decreased expression in cloned 2-cell embryos and were enriched in "intracellular protein transport" and "ubiquitin mediated proteolysis". In blastocysts, 593 genes showed decreased expression in cloned blastocysts and were enriched in "RNA binding", "nucleotide binding", "embryo development", and "adherens junction". We identified 14 development related genes that were not activated in the cloned embryos. Then, 68 and 245 long non-coding RNAs were recognized abnormally expressed in cloned 2-cell embryos and cloned blastocysts, respectively. Furthermore, we found that incomplete RNA-editing occurred in cloned embryos and might be caused by decreased ADAR expression. In conclusion, our study revealed the abnormal transcripts and deficient RNA-editing sites in cloned embryos and provided new data for further mechanistic studies of somatic nuclear reprogramming. The inhibitory activity of taxifolin on three digestive enzymes were investigated in both vitro and vivo. Taxifolin exhibited inhibitory effect on α-glucosidase, α-amylase and pancreatic lipase with IC50 values of 0.038, 0.647 and 0.993 mg/mL, respectively. Inhibitory kinetics indicated that taxifolin was more like a competitive inhibitor of α-glucosidase and α-amylase, while it was a non-competitive inhibitor of pancreatic lipase. The binding of taxifolin caused the quenching of intrinsic fluorescence intensity of enzymes, and the binding constant (lgKa) and the number of binding site (n) were further calculated through fluorescence titration. The values of lgKa were in the range of 4.93-6.65, and the values of n were all close to 1. Molecular docking indicated that taxifolin could interact with α-glucosidase and α-amylase through many kinds of secondary interaction, such as hydrogen bond, π-π stack, etc. In vivo study revealed that pre-administration with taxifolin can significantly improve the postprandial hyperglycemia in rat.