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Avidin biotin analysis

Q Yang, X-Y Liu, S-i Ajiki, M Hara, P Lundahl, J Miyake. Avidin-biotin immobilization of unilamellar liposomes in gel beads for chromatographic analysis of drug-membrane partitioning. J Chromatogr B 707 131-141, 1998. [Pg.186]

X-Y Liu, Q Yang, C Nakamura, J Miyake. Avidin-biotin-immobilized liposome column for chromatographic fluorescence on-line analysis of solute-membrane interactions. J Chromatogr B 750 51-60, 2001. [Pg.186]

Bayer EA, Wilchek M (1980) In Click D (ed.) Methods of biochemical analysis, vol. 26. Wiley, New York, p 1 Savage MD, Mattson G, Desai S, Nielander GW, Morgensen S, Conklin EJ (1992) Avidin-biotin chemistry a handbook. Pierce Chem. Comp., Rockford, Illinois, p 273... [Pg.122]

E. A. Bayer and M. Wilchek, The Use of the Avidin-biotin Complex as a Tool in Molecular Biology, in Methods of Biochemical Analysis (ed. D. Glick), John Wiley, New York, 1980, pp. 1-45. [Pg.111]

Masson et al. described a bioaffinity Pz sensor for biotin [174]. The sensor was based on the displacement of avidin from the crystal surface, which caused a large frequency increases when biotin was added to the solution. The surface was easily regenerated by addition of more avidin after analysis. [Pg.273]

Immunochemical analysis is a fast developing field with numerous possibilities for further improvement. Much effort is being put into the development of continuous measurements, such as flow-injection immunoanalysis (FI I A) and immunosensors. A quasicontinuous FI IA of pesticides was developed by Kramer and Schmid ) on the basis of a competitive lA. Here, the Abs are immobilized on a membrane. The reaction takes place in the membrane reactor, the central part of the flow injection system. All reagents are sequentially added to the reactor and the product is assayed with the aid of a fiow fiuorimeter. The measuring range of the fiow injection analysis almost equals that of the EIA. Wittmann and Schmid used an Ab column reactor filled with polystyrene or glass beads with the Ab immobilized via the avidin/biotin system. This system showed a stable Ab activity for a minimum of 500... [Pg.15]

Gychc voltammetry allows the analysis of the kinetics of the two integrated systems described earlier. Figure 11 shows the case of the avidin-biotin system (Sch. 5) where the voltammogram passes from a reversible surface wave shape to a plateau shape upon addition of glucose and where the inverse of the plateau current varies linearly with the inverse of glucose concentration. Similar data are obtained with the antigen-antibody... [Pg.5996]

A few years later egg-white injury in chicks was shown to be associated with a deficiency of biotin in the tissues, despite its abundance in the diet [145]. In the same year, avidin was isolated from egg-white and its ability to inactivate biotin in vitro was demonstrated [146]. Gyorgy and Rose [235] fed rats with avidin but only found very small amounts of biotin in the faeces until the faeces were steamed. Biotin was then released from the avidin-biotin complex. As the result of further experiments, it was concluded that the fundamental cause of egg-white injury is the unavailability of biotin due to its fixation to avidin, so that biotin is not absorbed from the intestinal tract and is excreted in the faeces [237]. A similar conclusion was reached by Sullivan and Nicholls [603] who showed that when egg-white is cooked, avidin is denatured and rendered incapable of binding biotin. Egg-white injury has been produced experimentally in man and can be cured by the administration of biotin [607]. In a recent study, Peters [497] reported that raw egg-white has a direct toxic effect which is not associated with its action in causing biotin deficiency. It would appear, therefore, that further studies on egg-white injury must be more closely associated with a critical analysis of the different components of egg-white. [Pg.344]

The proteins, avidin and streptavidin, are widely utilized in biotin analysis due to their outstanding aiSnity and specificity toward the binding of biotin (Zempleni et al. 2009). Generally an avidin-binding assay for the determination of biotin operates through the competition of sample biotin and labelled biotin (such as isotope-labelled biotin or biotinylated enzyme) with the limited number of avidin. Finally, the signals are acquired spectrophotometrically or electrochemically from the reaction of labelled enzyme with corresponding substrate or based on radioactivity counts. [Pg.387]

Bayer, E.A. and Wilchek, M. (1980) The use of the avidin-biotin complex as a tool in molecular biology. Methods of Biochemical Analysis, 26, 1-45. [Pg.157]

Anicet, A., Bourdillon, C., Moiroux, J., Savdant, J.-M. Step-by-step avidin-biotin construction of bienzyme electrodes. Kinetic analysis of the coupling between the catalytic activities of immobihzed mono-molecular layers of glucose oxidase and hexokinase. Langmuir 1999,15, 6527-6533. [Pg.272]

The determination of the lysozyme activity using the bacterial electrode (see p. 139) can also be used for immuno-analysis of biotine and avidine. The determination is based on the inhibition reaction of avidine with the biotine-lysozyme conjugate. After the reaction, the conjugate is no longer capable of dissolving the cell wall of the bacteria. The determination of biotine is similar [15]. [Pg.205]


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See also in sourсe #XX -- [ Pg.355 , Pg.356 , Pg.381 , Pg.383 , Pg.384 , Pg.386 , Pg.721 ]




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