Buffer dependence of refractive index increments of protein solutions

Ball, Vincent; Ramsden, Jeremy J.

doi:10.1002/(sici)1097-0282(199812)46:7<489::aid-bip6>3.0.co;2-e

Cited by 149 publications

(110 citation statements)

References 12 publications

Supporting

Mentioning

105

Contrasting

Unclassified

Order By: Relevance

“…GlOx adsorption was determined with Plasmos SD 2300 ellipsometer (PLASMOS GmbH, Munich, Germany [18,19,20,21]. Therefore, to simplify the model, the thickness of adsorbed layers was calculated using a planar isotropic model that assumed a refractive index of 3.865 for silicon and 1.450 for all the other layers.…”

Section: Evaluation Of Glutamate Oxidase Immobilizationmentioning

confidence: 99%

Glutamate detection by amino functionalized tetrahedral amorphous carbon surfaces

Kaivosoja

Tujunen

Jokinen

et al. 2015

Talanta

View full text Add to dashboard Cite

In this paper, a novel amperometric glutamate biosensor with glutamate oxidase (GlOx) immobilized directly on NH2 functionalized, platinum doped tetrahedral amorphous carbon (ta-C) film, has been successfully developed. First, we demonstrate that direct GlOx immobilization is more effective on amino-groups than on carboxyl-or hydroxyl-groups. Second, we show that anodizing and plasma treatments increase the amount of nitrogen and the proportion of protonated 2 amino groups relative to amino groups on the aminosilane coating, which subsequently results in an increased amount of active GlOx on the surface. This effect, however, is found to be unstable due to unstable electrostatic interactions between GlOx and NH3 + . We demonstrate the detection of glutamate in the concentration range of 10 µM−1mM using the NH2 functionalized Pt doped ta-C surface. The biosensor showed high sensitivity (2.9 nA μM -1 cm -2 ), low detection limit (10 μM) and good storage stability. The electrode response to glutamate was linear in the concentrations ranging from10 µM to 500 µM. In conclusion, the study shows that GlOx immobilization is most effective on aminosilane treated ta-C surface without any pre-treatments and the fabricated sensor structure is able to detect glutamate in the micromolar range.

show abstract

Section: Evaluation Of Glutamate Oxidase Immobilizationmentioning

confidence: 99%

Glutamate detection by amino functionalized tetrahedral amorphous carbon surfaces

Kaivosoja

Tujunen

Jokinen

et al. 2015

Talanta

View full text Add to dashboard Cite

show abstract

“…For the majority of soluble proteins dn/dc has approximately the same value (around 0.187 ml/g, the precise value depending on the buffer composition [13,14]) and is constant over a wide range of the protein concentrations. dn/dc may be determined experimentally using both a differential refractometer, which measures the difference in refractive index (DRI) between the macromolecular solution and the buffer, and a concentration sensitive detector:…”

Section: Soluble Proteinsmentioning

confidence: 99%

“…(17)). We use standard proteins to determine experimentally (dn/dc) protein , because the value is dependent on the buffer composition [13,14]. If the amount of attached detergent needs to be determined accurately, (dn/dc) detergent must be determined in the same buffer as used in the measurement too.…”

Section: Why Use Standards?mentioning

confidence: 99%

Static light scattering to characterize membrane proteins in detergent solution

Slotboom

Duurkens

Olieman

et al. 2008

Methods

167

176

View full text Add to dashboard Cite

“…A dn/dc value of 0.18 cm 3 /g was used, a value commonly used for protein adsorption [12]. For the silicon substrate, spectral refractive index data from WVASE were used.…”

Section: Spectroscopic Ellipsometrymentioning

confidence: 99%

Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry

Berlind

Poksinski²,

Tengvall

et al. 2010

Colloids and Surfaces B: Biointerfaces

View full text Add to dashboard Cite

Thick matrices of fibrinogen with incorporation of a matrix metalloproteinase inhibitor were covalently bonded on functionalized silicon surfaces using an ethyl-3-dimethyl-aminopropyl-carbodiimide and N-hydroxy-succinimide affinity ligand coupling chemistry. The growth of the structure was followed in situ using dynamic ellipsometry and characterized at steady-state with spectroscopic ellipsometry. The growth was compared with earlier work on ex situ growth of fibrinogen layers studied by single wavelength ellipsometry. It is found that in situ growth and ex situ growth yield different structural properties of the formed protein matrix. Fibrinogen matrices with thicknesses up to 58 nm and surface mass densities of 1.6 μg/cm 2 have been produced.

show abstract

Buffer dependence of refractive index increments of protein solutions

Abstract: The refractive index increment of a protein solution is a property not only of the protein, but also of the solvent. This is demonstrated theoretically and confirmed experimentally using analytical interferometry. © 1998 John Wiley & Sons, Inc. Biopoly 46: 489–492, 1998

Cited by 149 publications

References 12 publications

Glutamate detection by amino functionalized tetrahedral amorphous carbon surfaces

Glutamate detection by amino functionalized tetrahedral amorphous carbon surfaces

Static light scattering to characterize membrane proteins in detergent solution

Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry

Contact Info

Product

Resources

About