Determination of the rate constants for the FK506 binding protein/rapamycin interaction using surface plasmon resonance: An alternative sensor surface for Ni2+–nitrilotriacetic acid immobilization of His-tagged proteins

2007 ◽  
Vol 371 (2) ◽  
pp. 250-252 ◽  
Author(s):  
Martin A. Wear ◽  
Malcolm D. Walkinshaw

2011 ◽  
Vol 94 (4) ◽  
pp. 1217-1226 ◽  
Author(s):  
Pathik Vyas ◽  
Anthony A O'kane ◽  
E Ager ◽  
S Crooks ◽  
C Elliott ◽  
...  

Abstract A collaborative study was conducted on an inhibition-based protein-binding assay using the Biacore Q™ biosensor instrument and the Biacore Qflex™ Kit Vitamin B12 PI. The samples studied included infant formula, cereals, premixes, vitamin tablets, dietary supplements, and baby food. The collaborative study, which involved 11 laboratories, demonstrated that the assay showed an RSDr of 1.59–27.8 and HorRat values for reproducibility of 0.34–1.89 in samples with levels ranging from ppm to ppb. The assay studied is a label-free protein binding-based assay that uses the principle of surface plasmon resonance (SPR) to measure the interaction between vitamin B12 and a specifc binding protein. A Biacore Q biosensor uses this principle to detect binding directly at the surface of a sensor chip with a hydrophilic gold-dextran surface. The instrument passes a mixture of prepared sample extract and binding protein solution across a covalently immobilized vitamin B12 chip surface, and the response is given as free-binding protein as the mixture binds to the immobilized surface. This technique uses the specifcity and robustness of the protein-ligand interaction to allow minimal sample preparation and a wide range of matrixes to be analyzed rapidly. The reagents and accessories needed to perform this assay are provided as the ready-to-use format “Qflex Kit Vitamin B12 PI.” The method is intended for routine use in the quantitative determination of vitamin B12 (as cyanocobalamin) in a wide range of food products, dietary vitamin supplements, and multivitamin premixes.



2012 ◽  
Vol 95 (2) ◽  
pp. 329-334 ◽  
Author(s):  
Pathik Vyas ◽  
Anthony A O'Kane ◽  
Dawn Dowell

Abstract At the “Standards Development and International Harmonization: AOAC INTERNATIONAL Mid-Year Meeting” on June 29, 2011, an Expert Review Panel (ERP) agreed to further examine AOAC Official MethodSM 2011.01, “Determination of Vitamin B12 by Surface Plasmon Resonance,” for use with infant formula and adult nutritionals. The original collaborative study was conducted using the Biacore Q™ biosensor instrument and the Biacore Q™ Qflex™ Kit Vitamin B12 Pl. Samples included in the study were infant formula, cereals, premixes, vitamin tablets, dietary supplements, and baby food. Eleven laboratories participated in the collaborative study. The results demonstrated a repeatability RSD (RSDr) of 1.59–27.8 and HorRat values for reproducibility of 0.34–1.89 in samples with levels ranging from ppm to ppb. The assay studied is a label-free protein binding-based assay that uses the principle of surface plasmon resonance to measure the interaction between vitamin B12 and a specific binding protein by passing a portion of the prepared sample extract combined with binding protein solution across a functionalized sensor chip. The response from the functionalized sensor chip is given as free-binding protein, as the mixture binds to the prepared surface of the chip. The ready-to-use Qflex Kit Vitamin B12 PI provides the reagents and accessories necessary to perform this assay. AOAC Method 2011.01 was approved by the AOAC Method Committee on Food Nutrition for Official First Action status, applicable to a wide range of food products, dietary supplements, and multivitamin premixes. After evaluation of the validation data available, an ERP agreed in June 2011 that the method meets standard method performance requirements, as articulated by the Stakeholder Panel on Infant Formula and Adult Nutritionals. The ERP granted the method First Action status, applicable to infant formula and adult/pediatric nutritional formula.





Photonics ◽  
2021 ◽  
Vol 8 (2) ◽  
pp. 41
Author(s):  
Najat Andam ◽  
Siham Refki ◽  
Hidekazu Ishitobi ◽  
Yasushi Inouye ◽  
Zouheir Sekkat

The determination of optical constants (i.e., real and imaginary parts of the complex refractive index (nc) and thickness (d)) of ultrathin films is often required in photonics. It may be done by using, for example, surface plasmon resonance (SPR) spectroscopy combined with either profilometry or atomic force microscopy (AFM). SPR yields the optical thickness (i.e., the product of nc and d) of the film, while profilometry and AFM yield its thickness, thereby allowing for the separate determination of nc and d. In this paper, we use SPR and profilometry to determine the complex refractive index of very thin (i.e., 58 nm) films of dye-doped polymers at different dye/polymer concentrations (a feature which constitutes the originality of this work), and we compare the SPR results with those obtained by using spectroscopic ellipsometry measurements performed on the same samples. To determine the optical properties of our film samples by ellipsometry, we used, for the theoretical fits to experimental data, Bruggeman’s effective medium model for the dye/polymer, assumed as a composite material, and the Lorentz model for dye absorption. We found an excellent agreement between the results obtained by SPR and ellipsometry, confirming that SPR is appropriate for measuring the optical properties of very thin coatings at a single light frequency, given that it is simpler in operation and data analysis than spectroscopic ellipsometry.







2006 ◽  
Vol 3 (4) ◽  
pp. 271-282 ◽  
Author(s):  
Shiming Lin ◽  
Adam Shih-Yuan Lee ◽  
Chih-Chen Lin ◽  
Chih-Kung Lee


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