Voiding behavior of mice in the Saline + NTF and <i>E.coli</i> + NTF groups.

<p>(A) Voiding frequency (number) at PID 1, 4, 7 and 14. (B) Volume per void (μl) at PID 1, 4, 7 and 14 (B). n = 13 of Saline + NTF (gray bar), n = 12 of <i>E.coli</i> + NTF (black bar).</p

Combined analysis of voiding frequency and average voided volumes.

<p>(A) When average voided volume and voiding frequency are plotted together, the upper left hand corner is the domain of low frequency high volume (LVHF) voiding. The limits of this domain can be defined by percentile cut-points. (B) Plot of voiding frequency and average volume per void (μl) for each mouse mice in the Saline + NTF (gray circle) and <i>E.coli</i> + NTF (black square) groups at PID 14 with the LVHF domain defined by the 50^th percentile of frequency and volume.</p

<i>E.coli 1677</i>-induced prostatic inflammation.

<p>Representative H&E stained sections of the DLP (A, C, E, G) and bladder (B, D, F, H) of mice in the Saline + NTF and <i>E.coli</i> + NTF groups at PID 2 and PID 14, respectively.</p

2D plot of voiding frequency and volume per void.

<p>Distribution of voiding frequency (number) and average volume per void (μl) for each mouse mice in the Saline + NTF (gray circle) and <i>E.coli</i> + NTF (black square) groups at (A) PID 1, (B) PID 4, (C) PID 7 and (D) PID 14. P-values were calculated by Multivariate Analysis (MANOVA). * statistically significant.</p

Bacterial titer of the bladder and prostate.

<p>Number of colonies per mg of tissue of the bladder and prostate of mice in the Naïve + NTF, Saline + NTF, <i>E.coli</i> + NTF and <i>E.coli</i> only groups at PID 2 and 14 (total n = 32, n = 4 for each group at each time-point).</p><p>Bacterial titer of the bladder and prostate.</p

Magnetorheological Elastomer Films with Tunable Wetting and Adhesion Properties

We fabricated magnetorheological elastomer (MRE) films consisting of polydimethyl­siloxane and various concentrations of fluorinated carbonyl iron particles. The application of a magnetic field to the MRE film induced changes in the surface morphology due to the alignment of the iron particles along the magnetic field lines. At low concentrations of iron particles and low magnetic field intensities, needle-like microstructures predominated. These structures formed more mountain-like microstructures as the concentration of iron particles or the magnetic field intensity increased. The surface roughness increased the water contact angle from 100° to 160° and decreased the sliding angle from 180° to 10°. The wettability and adhesion properties changed substantially within a few seconds simply upon application of a magnetic field. Cyclical measurements revealed that the transition was completely reversible

Facile and Sensitive Method for Detecting Cardiac Markers using Ubiquitous pH Meters

A sensitive and easy method was developed for the detection of the cardiac marker troponin I using magnetic immunoassay and ubiquitous pH meters. Monoclonal antibody-functionalized Fe₃O₄ magnetic nanoparticle clusters (MNCs) were synthesized to capture troponin in human serum, and MNC–troponin complexes were magnetically isolated using a permanent magnet. These complexes were subsequently conjugated to polyclonal antibody-functionalized acetylcholinesterase (AchE) and dispersed in acetylcholine (Ach) solution. As the Ach was hydrolyzed to choline and acetic acid, the pH of the solution decreased, and the resulting pH change was measured in real time using a pH meter. The sensitivity of detection of this assay was found to be 10 pg/mL of troponin in human serum after 10 min of the hydrolysis reaction. Further, the pH change could be determined with the naked eye from the color change of a pH indicator strip

Investigation of Specific Binding Proteins to Photoaffinity Linkers for Efficient Deconvolution of Target Protein

Photoaffinity-based target identification has received recent attention as an efficient research tool for chemical biology and drug discovery. The major obstacle of photoaffinity-based target identification is the nonspecific interaction between target identification probes and nontarget proteins. Consequently, the rational design of photoaffinity linkers has been spotlighted for successful target identification. These nonspecific interactions have been considered as random events, and therefore no systematic investigation has been conducted regarding nonspecific interactions between proteins and photoaffinity linkers. Herein, we report the protein-labeling analysis of photoaffinity linkers containing three photoactivatable moieties: benzophenone, diazirine, and arylazide. Each photoaffinity linker binds to a different set of proteins in a structure-dependent manner, in contrast to the previous conception. The list of proteins labeled by each photoaffinity linker was successfully used to eliminate the nonspecific binding proteins from target candidates, thereby increasing the success rate of target identification

Investigation of Specific Binding Proteins to Photoaffinity Linkers for Efficient Deconvolution of Target Protein

Photoaffinity-based target identification has received recent attention as an efficient research tool for chemical biology and drug discovery. The major obstacle of photoaffinity-based target identification is the nonspecific interaction between target identification probes and nontarget proteins. Consequently, the rational design of photoaffinity linkers has been spotlighted for successful target identification. These nonspecific interactions have been considered as random events, and therefore no systematic investigation has been conducted regarding nonspecific interactions between proteins and photoaffinity linkers. Herein, we report the protein-labeling analysis of photoaffinity linkers containing three photoactivatable moieties: benzophenone, diazirine, and arylazide. Each photoaffinity linker binds to a different set of proteins in a structure-dependent manner, in contrast to the previous conception. The list of proteins labeled by each photoaffinity linker was successfully used to eliminate the nonspecific binding proteins from target candidates, thereby increasing the success rate of target identification

Sorbic, benzoic and propionic acids in fishery products: a survey of the South Korean market

<p>This study was conducted to provide basic data as part of a project to distinguish naturally occurring organic acids from added preservatives. Accordingly, we investigated naturally occurring levels of sorbic, benzoic and propionic acids in fish and their processed commodities. The levels of sorbic, benzoic and propionic acids in 265 fish and their processed commodities were determined by high-performance liquid chromatography–photodiode detection array (HPLC-PDA) of sorbic and benzoic acids and gas chromatography-mass spectrometry (GC/MS) of propionic acid. For propionic acid, GC-MS was used because of its high sensitivity and selectivity in complicated matrix samples. Propionic acid was detected in 36.6% of fish samples and 50.4% of processed fish commodities. In contrast, benzoic acid was detected in 5.6% of fish samples, and sorbic acid was not detected in any sample. According to the Korean Food and Drug Administration (KFDA), fishery products and salted fish may only contain sorbic acid in amounts up to 2.0 g kg⁻¹ and 1.0 g kg⁻¹, respectively. The results of the monitoring in this study can be considered violations of KFDA regulations (total 124; benzoic acid 8, propionic acid 116). However, it is difficult to distinguish naturally generated organic acids and artificially added preservatives in fishery products. Therefore, further studies are needed to extend the database for distinction of naturally generated organic acids and added preservatives.</p