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Haemoglobin Immobilization

Q.L. Wang, G.X. Lu, and B.J. Yang, Hydrogen peroxide biosensor based on direct electrochemistry of haemoglobin immobilized on carbon paste electrode by a silica sol-gel film. Sens. Actuators, B Chem. 99, 50-57 (2004). [Pg.601]

J.D. Zhang and M. Oyama, A hydrogen peroxide sensor based on the peroxidase activity of haemoglobin immobilized on gold nanoparticles-modified ITO electrode. Electrochim. Acta 50, 85-90 (2004). [Pg.603]

A. Salimi, E. Sharifi, A. Noorbakhsh, and S. Soltanian. Direct voltammetry and electrocatalytic properties of haemoglobin immobilized on a glassy carbon electrode modified with nickel oxide nanoparticles. Electrochem. Commun. 8, 1499-1508 (2005). [Pg.603]

Fig. 27. Dissociation curves for /) oxyhaemoglobin in solution 2) oxyhaemoglobin in human red cells and 3) immobilized haemoglobin. 37 °C, pH 7.4 pC02 40 Torr, p02 0-150 Torr... Fig. 27. Dissociation curves for /) oxyhaemoglobin in solution 2) oxyhaemoglobin in human red cells and 3) immobilized haemoglobin. 37 °C, pH 7.4 pC02 40 Torr, p02 0-150 Torr...
Table 12. Parameters of reversible oxygen transport for haemoglobin and a microdisperse form of immobilized haemoglobin (pH 7.4, 37 °C, pC02 = 40 Torr, p02 = 0-150 Torr)... Table 12. Parameters of reversible oxygen transport for haemoglobin and a microdisperse form of immobilized haemoglobin (pH 7.4, 37 °C, pC02 = 40 Torr, p02 = 0-150 Torr)...
Immobilized haemoglobin (Hb) was applied by Liu and co-authors (Liu et al. 2006) to the dehalogenation of haloethanes (hexachloroethane, pentachloro-ethane, tetrachloroethane, etc.). The observed fast electron-transfer reactions observed in aqueous-organic solvents are promising for the detection of the... [Pg.295]

Liu, H.-H., Wan, Y.-Q. and Zou, G.-L. (2006) Direct electrochemistry and electrochemical catalysis of immobilized haemoglobin in an ethanol-water mixture. Anal. Bioanal. Chem. 385, 1470-1476. [Pg.302]

The large three-dimensional structure of Hb, the resulting inaccessibihty of the heme centre, and the subsequent electrode passivation due to protein adsorption make it difficult to obtain DET between Hb and electrodes. Numerous efforts have been made to improve the electron transfer characteristics by using mediators or promoters [163]. The most efficient way is to modify preferentially carboneous electrodes with polymeric and membrane forming films, for example, surfactants [38], clay [57], and composite films of surfactant and bentonite. The redox potential of immobilized haemoglobin was determined between - 100 and - 380 mV vs. SCE. [Pg.288]

Open tubular capillary microreactor Trypsin Covalent linking IMER in fused silica capillaries integrated with nano-electrospray emitter trypsin immobilized on surface of the inner wall of the fused silica capillary tubing fast on-line digestion and peptide mass mapping of angiotensin II, Cyt-C, haemoglobin, and p-casein [118]... [Pg.319]

Open tubular capillary microreactor Pepsin Covalent linking Dextran-modified fused silica capillaries with immobilized trypsin Flow dependent digestion observed for native haemoglobin Flow rate [119]... [Pg.319]

The main problem of protein SERS study is that the protein native structure can be disturbed by its interaction with a metal surface. SERS spectra of oxy- and deoxy- haemoglobin indicated a partial denaturation of haemoglobin when adsorbed on Ag colloidal NPs (Smulevich and Spiro 1985). Biocompatible coating of the metal surface by SAMs of alkanethiols terminated with NH2- or COOH- groups mediating protein immobilization was used to preserve its native structure (Murgida and Hildebrandt 2006). Another way to keep the natural protein structure is the preparation of a specific SERS-active substrate where the protein molecule is more... [Pg.106]


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Haemoglobin

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