Silicon Nanowire Lab on a Chip

High sensitivity refractive index sensor based on micro-fiber with micro-arched transition

The osmotic pressure of concentrated protein solutions: Effect of concentration and ph in saline solutions of bovine serum albumin

Concentrated Aqueous Protein Systems, Proton Relaxation Times, Slow Chemical Exchange In this paper we present proton spin-lattice (T1) and spin-spin (T2) relaxation times measured vs. concentration, temperature, pulse interval (tauCPMG) as well as 1H NMR spectral measurements in a wide range of concentrations of bovine serum albumin (BSA) solutions. The anomalous relaxation behaviour of the water protons, similar to that observed in mammalian lenses, was found in the two most concentrated solutions (44% and 46%). The functional dependence of the spin-spin relaxation time vs. tauCPMG pulse interval and the values of the motional activation parameters obtained from the temperature dependencies of spin-lattice relaxation times suggest that the water molecule mobility is reduced in these systems. The slow exchange process on the T2 time scale is proposed to explain the obtained data. The proton spectral measurements support the hypothesis of a slow exchange mechanism in the highest concentrated solutions. From the analysis of the shape of the proton spectra the mean exchange times between bound and bulk water proton groups (tauex) have been estimated for the range of the highest concentrations (30%-46%). The obtained values are of the order of milliseconds assuring that the slow exchange condition is fulfilled in the most concentrated samples.

Relationship between SH group reactivity and concentration of bovine serum albumin and rat plasma

We demonstrated modulation of the waveguide mode mismatch via liquid cladding of the controllable refractive index for label-free quantitative detection of concentration of chemical or biological substances. A multimode optical fiber with its core exposed was used as the sensor head with the suitable chemical modification of its surface. Injected analyte liquid itself formed the liquid cladding for the waveguide. We found that modulation of the concentration of analyte injected enables a degree of the waveguide mode mismatch to be controlled, resulting in sensitive change in optical power transmission, which was utilized for its real-time quantitative assay. We applied the device to quantitating concentration of glycerol and bovine serum albumin (BSA) solutions. We obtained experimentally the limit of detection (LOD) of glycerol concentration, 0.001% (volume ratio), corresponding to the resolvable index resolution of ∼1.02 × 10-6 RIU (refractive index unit). The presented sensors also exhibited reasonably good reproducibility. In BSA detection, the sensor device response was sensitive to change in the refractive indices not only of liquid bulk but also of layers just above the sensing surface with higher sensitivity, providing the LOD experimentally as ∼3.7 ng/mL (mass coverage of ∼30 pg/mm2). A theoretical model was also presented to invoke both mode mismatch modulation and evanescent field absorption for understanding of the transmission change, offering a theoretical background for designing the sensor head structure for a given analyte. Interestingly, the device sensing length played little role in the important sensor characteristics such as sensitivity, unlike most of the waveguide-based sensors. This unraveled the possibility of realizing a highly simple structured label-free sensor for point-of-care testing in a real-time manner via an optical waveguide with liquid cladding. This required neither metal nor dielectric coating but still produced sensitivity comparable to those of other types of label-free sensors such as plasmonic fiber ones.

This paper reports that at a newly constructed small-angle x-ray scattering station of Beijing Synchrotron Radiation Facility, the topological shape of ligand-free bovine serum albumin in solution has been investigated. An appropriate scattering curve is obtained and the calculated value of the gyration radius is 31.2ű0.25A (1Å=0.1 nm) which is coincident with other ones' results. It finds that the low-resolution structure models obtained by making use of ab initio reconstruction methods are fitting the crystal structure of human serum albumin very well. All of these results perform the potential of the beamline to apply to structural biology studies. The characteristics, the defects, and the improving measures of the station in future are also discussed.

Formation of a carbonaceous film on the surface of Cu in a bovine serum albumin solution

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDielectric behavior of aqueous solutions of bovine serum albumin from radiowave to microwave frequenciesEdward H. Grant, Susan E. Keefe, and Shiro TakashimaCite this: J. Phys. Chem. 1968, 72, 13, 4373–4380Publication Date (Print):December 1, 1968Publication History Published online1 May 2002Published inissue 1 December 1968https://doi.org/10.1021/j100859a004RIGHTS & PERMISSIONSArticle Views249Altmetric-Citations67LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (814 KB) Get e-Alerts

Catalytic currents of albumin at the hanging mercury drop electrode

Ternary phase diagrams (TPDs) for aqueous bovine serum albumin (BSA) solutions containing ethanol or (NH4)2SO4 were determined for temperatures ranging from 20 to 70 degrees C. At 20 degrees C, ethanol destabilized BSA, resulting in gel formation at moderate solute concentrations. In contrast, (NH4)2SO4 concentrations above 20 wt % precipitated BSA from solution. Raising the temperature led to gel formation at increasingly lower BSA and solute concentrations. The removal of adsorbed fatty acids from BSA had little effect on the ethanol TPDs but reduced protein solubility in (NH4)2SO4. Moreover, the salt TPDs of fatty-acid-poor BSA were similar to those previously observed with S-ovalbumin.

The potential of using two natural polymers (chitosan and shellac) for the formation of nanoparticles by the process of ionic cross-linking to encapsulate bovine serum albumin, a model protein was investigated. Depending on the concentrations of chitosan, shellac and bovine serum albumin, three physical states – nanoparticle, aggregation, and solution could be observed as a result of the electrostatic force. The formation of nanoparticles was due to the balance between the repulsion force and attractive force while the imbalance between both forces resulted in the formation of aggregation and solution. The Fourier transform infrared spectroscopy and differential scanning calorimetry were applied to prove the nanoparticle formation. The particle size was characterized by the light scattering technique and was found in the range between 100 and 300 nm. The morphology of the particles, detected by transmission electron microscopy was spherical shape. The result showed that the zeta potential of the nanoparticles possessed positive charges. The concentrations of chitosan, shellac and bovine serum albumin had an influence on the physicochemical properties of the nanoparticles such as the particle size, the zeta potential, the encapsulation, the loading efficiencies and the cumulative release. Therefore, chitosan and shellac could be used to form nanoparticles for protein delivery by the ionic cross-linking method.

Effect of Freezing Rate and Dendritic Ice Formation on Concentration Profiles of Proteins Frozen in Cylindrical Vessels

In this study, we firstly investigated the surface and protein adsorption properties of montmorillonite (MMT)/chitosan (CS) composite films with various MMT/CS weight ratios for metallic implants coating applications. Bicinchoninic acid (BCA) protein assay results show that the neat CS film exhibits a high concentration of bovine serum albumin (BSA) protein adhesion because the abundant carbonyl and amide functional groups on the surface of the CS film easily form hydrogen bonds with the copious carboxylic acid groups on the surface of the BSA protein. The MMT/CS composite films with MMT/CS = 3, 5, 8, and 10 possess a much lower BSA adhesion concentration than that of the neat CS film, as some of the carbonyl and amide functional groups on the surface of the composite films are replaced by the –Si–O–Si and –Al–O–Al groups. Among these MMT/CS composite films, the film with MMT/CS = 5 exhibits the lowest BSA adsorption concentration because it possesses a higher MMT content than those with MMT/CS = 1 and 3 and a smoother and non-porous surface than those with MMT/CS = 8 and 10. According to our results, MMT/CS composite films with appropriate MMT/CS weight ratios exhibit better surface and protein adsorption properties than neat CS for biomedical applications.

Surface characteristics of the 316L stainless steel modified by ethylene vinyl acetate/chitosan composite films

Voltea invests in US robotic production plant