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#29054385   2017/10/21 Save this To Up

Functionalized Calcium Carbonate Microparticles for the Delivery of Proteins.

The recently introduced functionalized calcium carbonate (FCC), a porous microparticle with a nano-structured, lamellar surface, shows promising properties in the field of oral drug delivery. In this work, FCC was loaded with biomolecules e.g. lysozyme (Lys) and bovine serum albumin (BSA) in order to investigate its suitability to deliver protein based drugs. Loading efficiency for our model proteins was >90%and enzyme activity was preserved as demonstrated by Michaelis-Menten enzyme kinetic experiments. Circular dichroism analysis confirmed, that neither the structure of both model substances, nor the activity of Lys was affected by the loading process or the interaction with the surface of FCC. Electron microscopy (SEM) and mercury porosimetry were indicative of protein deposition on the particle surface as well as within the particle pores. Release properties were investigated in a customized flow cell, which simulates the conditions in the oral cavity. Depending on the isoelectric point of the investigated proteins, complete release was obtained within 1.5 hours. This work shows, that FCC is a suitable pharmaceutical excipient for delivery of proteins.

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Recombinant Human PKC the Recombinant Human PKC the Recombinant Human PKC the Calcium carbonate CAS Num Native Human Lactoferrin, Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media Calcium Stain Kit (Modif Calcium Stain Kit (Modif

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#29053706   2017/10/20 Save this To Up

Solea senegalensis sperm cryopreservation: New insights on sperm quality.

Cryopreservation of Senegalese sole sperm can represent an alternative to overcome some reproductive problems of this species. However, it is important to guarantee the safe use of cryopreserved sperm by selecting an appropriate protocol according to a high demand quality need to be ensured. It has been demonstrated that traditional assays such as motility and viability do not provide enough information to identify specific damage caused by cryopreservation process (freezing and thawing). Specific tests, including lipid peroxidation and DNA damage, should be performed. In the present study, motility and lipid peroxidation were performed as specific tests allowing us to discard cryopreservation conditions such as methanol as internal cryoprotectant and bovine serum albumin as external cryoprotectant. In addition, a caspase 3/7 detection by flow cytometry was performed to analyze apoptosis activity in the best selected conditions. Moreover, new highly sensitive tests based on transcript number detection have recently been described in fish sperm cryopreservation. For this reason, a transcript level detection assay was performed on certain oxidative and chaperone genes related to fertilization ability and embryo development (hsp70, hsp90BB, hsp90AA, gpx) to select the best cryopreservation conditions. DMSO+ egg yolk proved to be the best cryoprotectant combination in terms of transcript level. This study describes an optimized cryopreservation protocol for Solea senegalensis sperm demonstrating for the first time that transcript degradation is the most sensitive predictor of cell status in this species after cryopreservation.

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Herring Sperm DNA Salmon Sperm DNA Spermidine CAS Number [12 Spermidine trihydrochlori Spermine CAS Number [71 4 Bcl-2 Oncoprotein; Clone Bcl-2 Oncoprotein; Clone c-erbB-2 Oncoprotein c-erbB-2 Oncoprotein c-erbB-3 Oncoprotein; Cl c-erbB-3 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl

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#29052335   2017/10/20 Save this To Up

A comparative study on intrinsic fluorescence of BSA and lysozyme proteins in presence of different divalent ions from their solution and thin film conformations.

Optical emission behaviours of lysozyme and bovine serum albumin, from bulk and thin film geometry, were studied in the presence of three different divalent ions (Mg(2+) , Ca(2+) or Ba(2+) ) using different spectroscopic [steady-state fluorescence, UV-Vis and Fourier transform infra-red (FTIR)] techniques. Additionally, protein thin films on silicon surfaces were prepared and morphological studies were carried out using atomic force microscopy. Dynamic quenching was mainly identified for both proteins in the presence of Mg(2+) , Ca(2+) and Ba(2+) ions. The molecular conformation of the proteins was modified in thin films compared with that in solution, consequently quenching efficiencies also varied. ATR-FTIR studies confirmed the conformational changes of proteins in the presence of all divalent ions. All metal ions used were divalent in nature and belonged to the same group of the periodic table but, depending on their individual characteristics such as electron affinity, ionic radius, etc., the magnitude of the protein and hydrated ion interaction varied and accordingly the quenching efficiency was modified. Quenching was maximum for Ca(2+) ions, followed by the other two ions. Our study clearly illustrates the geometry-dependent physical and biological functions of proteins.

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#29052332   2017/10/20 Save this To Up

Effect of different extenders for donkey sperm vitrification in straws.

Aseptic vitrification of semen samples packed in straws has been successfully developed in human but not in donkeys. The aim of this study was to compare the effect of two extenders for donkey sperm vitrification using straws. Ejaculates from four Andalusian donkeys were collected, and samples were extended in INRA-96 (I) or Gent (G) supplemented with sucrose 0.25 M and 1% bovine serum albumin (BSA). Extended samples were cooled for one hour at 5°C. For vitrification, samples were filled in covered 0.25 ml straws and then plunged directly into liquid nitrogen. For warming, straws were immersed in INRA-96 at 43°C. Results showed no significant differences between I and G treatments for TM (34.2% ± 8.7 vs. 30.7% ± 9.6) and PM (26.8% ± 7.3 vs. 24.6% ± 7.9), respectively. In conclusion, donkey sperm could be vitrified in straws either with INRA-96 or with Gent in combination with sucrose and BSA.

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#29051637   2017/10/20 Save this To Up

Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin.

In this study, theaflavins (TF1, TF2A, TF2B and TF3) were prepared from black tea and their interaction with bovine serum albumin (BSA) was explored by fluorescence and CD spectroscopy. The results showed that the structures of theaflavins exhibited significant effects on the binding/quenching process, and the binding affinity increased with the increase of molecular weight of theaflavins and the presence of galloyl moiety. The quenching effects showed a sequence as TF3 > TF2A > TF2B > TF1, demonstrating the important role of the galloyl moiety on the C-3 position of theaflavins. CD spectra indicated that TF3 in high concentration could change the skeleton structure of BSA and induce the unfolding of BSA secondary structure. The present results provide a new perspective for better understanding of the likely physiological fate of theaflavins and help to control the functional characteristics of food.

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Bovine Serum Albumin (BSA Bovine Androstenedione,AS Bovine serum albumin Bovine serum albumin Anti Anti-Bovine Serum Albumin Anti Bovine Serum Albumin Anti-Bovine Serum Albumin Monoclonal Anti-Bovine Se Monoclonal Anti Bovine Se BSA | bovine serum albumi BSA | bovine serum albumi BSA | bovine serum albumi

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#29050583   2017/10/20 Save this To Up

Characterization, antioxidant property and cytoprotection of exopolysaccharide-capped elemental selenium particles synthesized by Bacillus paralicheniformis SR14.

Instead of using existing methods to chemically synthesize elemental selenium particles (CheSePs), which first require separating and purifying polysaccharides or proteins and adding extra reducing agent, this study applied a novel method to directly assemble exopolysaccharide-capped biogenic elemental selenium particles (EPS-BioSePs) by Bacillus paralicheniformis SR14 during the metabolic process. Characterization by energy dispersive X-ray spectrometry (EDX), scanning electron microscopy (SEM), transmission electron microscopy (TEM), X-ray photoelectron spectroscopy (XPS), Fourier transform infrared spectroscopy (FT-IR), size measurement and chemical composition analysis verified that EPS-BioSePs exhibited a monodispersed and homogeneous spherical structure 293.73±4.03nm in size. Compared to a widely used form of CheSePs stabilized and coated by bovine serum albumin, EPS-BioSePs exhibited better antioxidant properties on scavenging DPPH, superoxide and ABTS free radicals, but not hydroxyl radical. In vitro experiments with porcine jejunum epithelial (IPEC-J2) cells also indicated a significant cytoprotection of EPS-BioSePs against hydrogen peroxide-induced oxidative stress, as exhibited by cell viability reduction and suppression of ROS generation. These results suggested that this new form of selenium possessed great antioxidant property and cytoprotection and exopolysaccharide-producing bacteria could gradually become an appropriate choice to synthesize biogenic elemental selenium particles with potential applications as antioxidants.

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Polystyrene Particles, 2 Streptavidin Coated Poly UltraRainbow Fluorescent BACILLUS CEREUS Z091, tit Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge

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#29048834   2017/10/19 Save this To Up

[Preparation and performance characterization of gold nanoparticles modified chiral capillary electrochromatography stationary phase].

Gold nanoparticles (GNPs, 15 nm) were prepared and introduced to amino groups derived silica monolithic column. Bovine serum albumin (BSA) was immobilized via covalent modification method onto the carboxylic functionalized GNPs to afford chiral stationary phase (CSP) for enantioseparation. GNPs were well dispersed and successfully incorporated onto the columns with the contents as high as 17.18% by characterization method such as transmission electron microscopy (TEM), ultraviolet (UV)-visible absorption spectra and scanning electron microscopy (SEM). The preparation conditions of the BSA modified CSP were optimized and 10% (v/v) 3-aminopropyltriethoxysilane (APTES) and 15 g/L BSA were selected as appropriate reaction conditions. The enantioseparation performance of the BSA modified CSP has been investigated by capillary electrochromatography (CEC). Enantiomers of tryptophan, ephedrine and atenolol were resolved, and the baseline separation of tryptophan was achieved. Meanwhile, the influences of pH value, buffer concentrations and applied voltages used on the chiral separation were studied, and the optimal separation conditions were 10 mmol/L phosphate buffer at pH 7.4 and 15 kV applied voltages. In comparison with the BSA modified CSP prepared by physical adsorption, the CSP prepared by covalent modification method had better separation results, and the analytes could be separated directly without pre-column derivatization. In addition, the prepared BSA modified CSP exhibited good run to run repeatability with relative standard deviations (RSDs) of the migration times and selectivity factors not more than 2.3% and 0.96%, respectively. This work offers a good thinking for modification with other proteins or other types of chiral selectors.

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Gram Stain Kit (Modified Calcium Stain Kit (Modif Calcium Stain Kit (Modif Elastic Stain Kit (Modif Elastic Stain Kit (Modif Gold Chloride Solution ( Gold Chloride Solution ( Gold Chloride Solution ( Gold Chloride Solution ( Gold Chloride Solution ( Gold Chloride Solution ( Reticulum Stain Kit (Mod

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#29045929   2017/10/18 Save this To Up

Deciphering the complexation process of a fluoroquinolone antibiotic, levofloxacin, with bovine serum albumin in the presence of additives.

The current work aims to explore the thermodynamic and conformational aspects for the binding of fluoroquinolone antibacterial drug, levofloxacin (LFC), with bovine serum albumin (BSA) using calorimetric, spectroscopic (UV-visible, fluorescence, circular dichroism, and (1)H NMR), dynamic light scattering (DLS) and computational methods (molecular docking). The binding of LFC with BSA at two sequential sites with higher affinity (~10(3)M(-1)) at the first site has been explored by calorimetry whereas the binding at a single site with affinity of the order of ~10(4)M(-1) has been observed from fluorescence spectroscopy. The calorimetric study in the presence of additives along with docking analysis reveals the significant role of electrostatic, hydrogen bonding, and hydrophobic interactions in the association process. The slight conformational changes in protein as well as the changes in the water network structure around the binding cavity of protein have been observed from spectroscopic and DLS measurements. The LFC induced quenching of BSA fluorescence was observed to be initiated mainly through the static quenching process and this suggests the formation of ground state LFC-BSA association complex. The stronger interactions of LFC in the cavity of Sudlow site I (subdomain IIA) of protein have been explored from site marker calorimetric and molecular docking study.

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Bovine Serum Albumin (BSA Thermal Shaker with cooli FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Multiple organ tumor tiss Bovine serum albumin Bovine serum albumin Anti Anti-Bovine Serum Albumin

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#29042926   2017/10/18 Save this To Up

Anti-EGFR antibody conjugated silica nanoparticles as probes for lung cancer detection.

A well-designed nanosystem [anti-epidermal growth factor receptor-MB-encapsulated thiol-terminated silica nanoparticles (EGFR/MB-SHSi) complexes] containing silica nanoparticles and near-infrared fluorescence dye (NIRF) methylene blue (MB) was established as a tumor-targeted probe for potential lung cancer detection. The anti-EGFR/MB-SHSi complexes exhibited desirable and homogenous particle size, high bovine serum albumin stability, low hemolytic activity, neutral surface charges and negligible cytotoxicity in vitro. Furthermore, the results of confocal laser scanning microscopy and flow cytometry confirmed that the EGFR-targeted function induced high and specific cellular uptake of anti-EGFR/MB-SHSi complexes. In vivo investigation of nude mice bearing A549 tumor xenografts revealed that anti-EGFR/MB-SHSi complexes possessed strong tumor target ability. These observations indicated that anti-EGFR/MB-SHSi complexes may be a safe and tumor-targeting probe for the detection of cancer.

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#29042638   2017/10/18 Save this To Up

Carbon nanowalls as a platform for biological SERS studies.

Herein we report about developing new type of Surface Enhanced Raman Scattering (SERS) substrates based on Au-decorated carbon nanowalls. The designed substrates possess high specific surface area and high sensitivity. Chemical stability of Au perfectly blends with electrical properties and high value of specific surface area of carbon nanowalls. Created structures were applied to detect signals of a typical molecule used for SERS substrates testing, rhodamine 6G, which exhibits electronic absorption in the visible area of spectrum, and biomacromolecules such as tryptophan, guanine, bovine serum albumin and keratin hydrolysates, whose electronic absorption is in the ultraviolet region of spectrum and lies far from the Au plasmonic resonance. The obtained signals for these compounds suggest that the developed substrate is a prominent platform for the detection of biological macromolecules. The properties of the substrate, including its morphology and Au film thickness, as well as the analyte deposition method, were optimized to achieve the optimum Raman signal enhancement. Electric field distribution in the designed structures was calculated to describe the observed dependence of SERS activity on the substrate morphology.

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