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361. Biosensor Research Group
Prussian Blue based selective electrocatalyst for hydrogen peroxide reduction (artificial peroxidase). Application to biosensors. ... A high sensitive glucose amperometric biosensor based on Prussian Blue modified electrodes. ... A first-generation amperometric glucose biosensor based on a Prussian Blue-modified electrode was developed. ... The glucose amperometric biosensor was made by glucose oxidase immobilization onto a Prussian Blue-modified electrode with a Nafion layer. ...
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Ссылки http://www.enzyme.chem.msu.ru/biosens/eng/publ.htm -- 19.7 Кб -- 22.02.1999
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362. Biosensor Research Group
Head: PhD, Dr.Sci. ... senior research scientist . ... PhD student . ... Fax: (7-095) 939 2742 , (7-095) 939 5417, . ... Research interest: development of novel electrochemical biosensors and immunosensors on the basis of conductive polymers, electroactive inorganic polycrystals and self-assembled multilayers. ... Prussian Blue based selective electrocatalyst for hydrogen peroxide reduction (artificial peroxidase). Application to biosensors. ... Application to dehydrogenase based biosensors. ...
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Ссылки http://www.enzyme.chem.msu.ru/biosens/eng/ -- 4.0 Кб -- 22.02.1999
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363. LABORATORY OF MICELLAR ENZYMOLOGY
LABORATORY OF MICELLAR ENZYMOLOGY . ... The main goal of the laboratory of micellar enzymology (it is now 10 years since the lab was announced) is studying the role of supramolecular organization of enzymes in their functioning. It was suggested for enzymes to be entrapped into surfactants aggregates, micelles, for modelling their natural biomembrane environment. Such aggregates can be formed in the systems surfactant-water-organic solvents. ...
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Ссылки http://www.enzyme.chem.msu.ru/micella/eng/ -- 3.7 Кб -- 22.02.1999
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364. http://www.enzyme.chem.msu.ru/~tishkov/Publications/BJ_FDH_97.pdf
... The value of Vmax, rate-limiting hydride transfer, is nearly constant throughout the entire pH range of enzyme stability (6.011.2) but decreases below 6. ... NAD+-dependent formate dehydrogenase (FDH ; formate : NAD+ oxidoreductase, EC 1.2.1.2) from the methylotrophic bacterium Pseudomonas sp. 101 (pFDH) is one of the most extensively characterized NAD+-dependent dehydrogenases. ... However, no carboxylic residues are in the vicinity of the formate-binding site in the crystal structure of pFDH. ...
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Ссылки http://www.enzyme.chem.msu.ru/~tishkov/Publications/BJ_FDH_97.pdf -- 541.4 Кб -- 24.01.1997
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