Physical modelling of backward erosion piping in levee foundation subjected to repeated flooding: (Abstract)

<p>The T-RFLP was based on Hae III (A) and MSP I (B) restriction enzymes. Cows were fed a control diet (CON) or a diet with 10% (10% FM) and 15% flax meal (15% FM). Scale relates to percent similarity and data are presented per period (Per).</p

Taxonomic identification of DGGE bands potentially associated with enterolactone production in ruminal fluid.

<p>Taxonomic identification of DGGE bands potentially associated with enterolactone production in ruminal fluid.</p

Pathway of enterolignans production from SDG by human faecal bacteria (Adapted from [8]).

<p>Pathway of enterolignans production from SDG by human faecal bacteria (Adapted from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0087949#pone.0087949-Clavel1" target="_blank">[8]</a>).</p

DGGE gel for sequencing purpose.

<p>This DGGE gel shows rumen bacterial diversity within cows fed no flax meal (CON) or 15% flax meal (15%) in the diet (dry matter basis). Arrows show bands that appeared upon flax meal supplementation, which were cut and sequenced.</p

Mean peak/band number following HaeIII- and MSP1-based 16S rRNA T-RFLP and V6–V8 PCR-DGGE of rumen bacteria within rumen samples obtained from Holstein cows fed a control diet with no flax meal (CON), 10% (10FM) and 15% (15FM) of flax meal (FM) in the dry matter.

<p>Mean peak/band number following HaeIII- and MSP1-based 16S rRNA T-RFLP and V6–V8 PCR-DGGE of rumen bacteria within rumen samples obtained from Holstein cows fed a control diet with no flax meal (CON), 10% (10FM) and 15% (15FM) of flax meal (FM) in the dry matter.</p

Concentration of enterolactone (µmol/L) in ruminal fluid of Holstein cows fed flax meal (FM).

<p>Cows were fed a control diet (CON) or a diet with 5% FM (5FM), 10% FM (10FM) and 15% FM (15FM). There was a linear effect of treatment (<i>P</i><0.0001) before feeding and in the post-feeding pool of ruminal fluid. The standard error was 0.001 for all sampling times.</p

Efficiency of conversion of SDG into SECO by selected pure cultures of ruminal bacteria and conversion of SDG into SECO and ED using ruminal fluid as inoculum, assessed using <i>in vitro</i> cultures and HPLC¹.

1<p>The HPLC results were converted into molarities (SDG <i>M</i> = 686.7 g/mol; SECO <i>M</i> = 362.4 g/mol; ED <i>M</i> = 302.36 g/mol), and expressed as the percentage, in relation to the initial concentration of SDG of 1.14 m<i>M</i>; n.d.: non-detected.</p

Ingredients and chemical composition of experimental diets.

<p>*Control diet with no flax meal (FM) or a diet with 5%, 10% and 15% FM (DM basis).</p>†<p>Contained 20% of canola meal, 30% of corn gluten meal, 20% of soybean meal, and 30% of brewer's corn.</p>‡<p>Contained 9.2% Ca; 4.79% P; 4.78% Mg; 1.52% S; 13.72% Na; 1.37% K; 19.5 mg/kg Se; 23 mg/kg I; 2013 mg/kg Fe; 1068 mg/kg Cu; 1796 mg/kg Mn; 2657 mg/kg Zn; 57 mg/kg Co; 265 mg/kg Fl; 442000 UI/kg vitamin A; 56670 UI/kg vitamin D; and 2630 UI/kg vitamin E.</p>¶<p>Values with standard errors of the mean.</p

Versatile <i>O</i>‑GlcNAc Transferase Assay for High-Throughput Identification of Enzyme Variants, Substrates, and Inhibitors

The dynamic glycosylation of serine/threonine residues on nucleocytoplasmic proteins with a single <i>N</i>-acetylglucosamine (<i>O</i>-GlcNAcylation) is critical for many important cellular processes. Cellular <i>O</i>-GlcNAc levels are highly regulated by two enzymes: <i>O</i>-GlcNAc transferase (OGT) is responsible for GlcNAc addition and <i>O</i>-GlcNAcase (OGA) is responsible for removal of the sugar. The lack of a rapid and simple method for monitoring OGT activity has impeded the efficient discovery of potent OGT inhibitors. In this study we describe a novel, single-well OGT enzyme assay that utilizes 6 × His-tagged substrates, a chemoselective chemical reaction, and unpurified OGT. The high-throughput Ni-NTA Plate OGT Assay will facilitate discovery of potent OGT-specific inhibitors on versatile substrates and the characterization of new enzyme variants

Fabrication and Characterization of Plasma-Polymerized Poly(ethylene glycol) Film with Superior Biocompatibility

A newly fabricated plasma-polymerized poly­(ethylene glycol) (PP-PEG) film shows extremely low toxicity, low fouling, good durability, and chemical similarity to typical PEG polymers, enabling live cell patterning as well as various bioapplications using bioincompatible materials. The PP-PEG film can be overlaid on any materials via the capacitively coupled plasma chemical vapor deposition (CCP-CVD) method using nontoxic PEG200 as a precursor. The biocompatibility of the PP-PEG-coated surface is confirmed by whole blood flow experiments where no thrombi and less serum protein adsorption are observed when compared with bare glass, polyethylene (PE), and polyethylene terephthalate (PET) surfaces. Furthermore, unlike bare PE films, less fibrosis and inflammation are observed when the PP-PEG-coated PE film is implanted into subcutaneous pockets of mice groin areas. The cell-repellent property of PP-PEG is also verified via patterning of mammalian cells, such as fibroblasts and hippocampal neurons. These results show that our PP-PEG film, generated by the CCP-CVD method, is a biocompatible material that can be considered for broad applications in biomedical and functional materials fields