@misc{KrauseMirskyHeckmann, author = {Krause, Christian and Mirsky, Vladimir M. and Heckmann, Klaus Dietrich}, title = {Capacitive detection of surfactant adsorption on hydrophobized gold electrodes}, series = {Langmuir}, volume = {12}, journal = {Langmuir}, number = {25}, issn = {0743-7463}, doi = {10.1021/la9601869}, pages = {6059 -- 6064}, abstract = {Nonspecific adsorption of surfactants on polycrystalline gold electrodes, covered by a chemically adsorbed monomolecular layer of octadecanethiol, was studied by means of capacitive measurements. Homologous series of fatty acids (from decane to tetradecane acids) and dodecanepyridinium chloride were used as surfactants. The behavior of the electrode was completely different in the first and subsequent cycles of adsorption/desorption. In the first adsorption cycle, an initial capacitance jump at low concentrations (<10 μM) occurs, while later the curves show the usual saturation behavior. The first surfactant layer could not be completely desorbed; only the electrode capacitance shown after the jump was reached. Subsequent cycles do not reveal any capacitance jumps and were completely reversible. Adsorption curves in the series of monoalkyl acids are shifted according to the Traube rule. A comparison with the surfactant adsorption at the air/water interface has been done.}, language = {en} } @misc{MirskyKrauseHeckmann, author = {Mirsky, Vladimir M. and Krause, Christian and Heckmann, Klaus Dietrich}, title = {Capacitive sensor for lipolytic enzymes}, series = {Thin Solid Films}, volume = {284-285}, journal = {Thin Solid Films}, issn = {0040-6090}, doi = {10.1016/S0040-6090(95)08485-1}, pages = {939 -- 941}, abstract = {The preparation of the capacitive biosensor for monitoring the activity of enzymes (lipases, phospholipases, etc.) hydrolysing waterinsoluble substrates into water-soluble products is described. The sensor is based on a sandwich-like structure: Au/S(CH₂)₁₇CH₁/substrate/electrolyte. Hydrolysis of the substrate leads to the formation of water-soluble products and desorption of these compounds from the electrode. When the product formation is the rate-limiting step of this process, the desorption rate is determined by the enzyme activity. The desorption can be easily monitored as an increase of the electrode capacitance. By following this principle it was possible to develop a sensor monitoring phospholipase A₂ activity even at the 50 pg ml-1 level.}, language = {en} } @misc{HayessenMirskyHeckmann, author = {Hayessen, R. and Mirsky, Vladimir M. and Heckmann, Klaus Dietrich}, title = {Anion-sensitive properties of alkylguanidines in the membrane electrodes and monomolecular layers}, series = {Sensors and Actuators B: Chemical}, volume = {32}, journal = {Sensors and Actuators B: Chemical}, number = {3}, issn = {0925-4005}, doi = {10.1016/S0925-4005(97)80032-9}, pages = {215 -- 220}, abstract = {Water-insoluble alkylguanidines and cycloguanidines (triphenyl-, tricyclohexyl- and tribenzylguanidines) have been synthesized and studied as potential nitrate ligands. Anion-dependent expansion of dialkylguanidinium monolayers at the water/air interface is observed; the area per guanidinium molecule in the monolayer increases according to the series I->NO3->Cl-. Membranes for nitrate-sensitive electrodes are prepared by immobilization of alkyl- and cycloguanidiniums into a plasticized polyvinylchloride matrix. Nernst-type dependence of the electrode potential on the nitrate concentration is observed for the electrodes prepared with long-chain alkylguanidines, and only a small response is observed for electrodes based on the cycloguanidines. The selectivity qualitatively follows the Hofmeister series: I->NO3->Br->F-. The effect of plasticizers on the dielectric constant of the membranes has been studied, and variations from 6.5 (dibutylphthalate) to 16 (tributylphosphate) are obtained. In spite of some quantitative variations of the electrode selectivity, the Hofmeister series is qualitatively valid for all the electrodes. No correlation between dielectric constant of the electrode membrane and electrode selectivity is observed.}, language = {en} } @misc{Mirsky, author = {Mirsky, Vladimir M.}, title = {Fatty acids effect on the phospholipase A: electrostatical mechanism of activation}, series = {Membrane and Cell Biology}, volume = {9}, journal = {Membrane and Cell Biology}, issn = {1023-6597}, pages = {175 -- 184}, language = {en} } @inproceedings{HayessenMirskyHeckmann, author = {Hayessen, R. and Mirsky, Vladimir M. and Heckmann, Klaus Dietrich}, title = {Alkylguanidines as a base for nitrate ion sensors}, series = {Sensor-95, Kongress-Band, 7. Internationale Fachmesse mit Kongreß f{\"u}r Sensoren, Meßaufnehmer \& Systeme, 9. - 11. Mai, N{\"u}rnberg}, booktitle = {Sensor-95, Kongress-Band, 7. Internationale Fachmesse mit Kongreß f{\"u}r Sensoren, Meßaufnehmer \& Systeme, 9. - 11. Mai, N{\"u}rnberg}, publisher = {ACS}, address = {Wunstorf-Steinhude}, pages = {841 -- 844}, language = {en} } @misc{Mirsky, author = {Mirsky, Vladimir M.}, title = {An effect of the lipid hydrolysis products on the phospholipase A₂ action towards lipid monolayer}, series = {Physics and Chemistry of Lipids}, volume = {70}, journal = {Physics and Chemistry of Lipids}, number = {1}, issn = {0009-3084}, pages = {75 -- 81}, abstract = {The effect of lauric acid (LA) and lysolauroyllecithin (LLL) on the hydrolysis of lipid in monolayer by phospholipase A₂ from Bee venom was studied. It was found that LLL inhibits phospholipase action under both high (39 mN/m) and low (25 mN/m) surface pressure. On the other hand, LA inhibits phospholipase action under the low surface pressure (15 mN/m or 25 mN/m), but increases enzyme activity under high surface pressure (39 mN/m). This activating effect can be suppressed by high ionic strength of the aqueous subphase. It is suggested that an increase of the negative surface charge of the lipid monolayer, followed by an increase of the local concentrations of the positively charged enzyme and calcium near the monolayer is a coupling factor between fatty acid accumulation and phospholipase activation. Such an autocatalytic process can only occur when the substrate is organised into monolayer, bilayer or micelles, therefore it can be considered as a reason for the substrate activation and induction time before lipid hydrolysis.}, language = {en} } @misc{StozhkovaMirskySokolov, author = {Stozhkova, I. N. and Mirsky, Vladimir M. and Sokolov, Valeri S.}, title = {Stoichiometry of the photochemical reaction leading to the damage of BLM in the presence of hematoporphyrin}, series = {Biological membranes}, volume = {10}, journal = {Biological membranes}, number = {1}, pages = {44 -- 49}, language = {en} } @misc{StozhkovaMirskyKayushinaetal., author = {Stozhkova, I. N. and Mirsky, Vladimir M. and Kayushina, R. L. and Erokhin, V. V. and Mironov, A. F.}, title = {An interaction of hematoporphyrin dimethylether with model lipid membranes}, series = {Biological membranes}, volume = {9}, journal = {Biological membranes}, number = {1}, pages = {74 -- 79}, language = {en} } @misc{StozhkovaMirskySzito, author = {Stozhkova, I. N. and Mirsky, Vladimir M. and Szito, T.}, title = {Photosensitized by hematoporphyrin dimethylether damage of bilayer lipid membrane}, series = {Biological membranes}, volume = {8}, journal = {Biological membranes}, number = {4}, issn = {0748-8653}, pages = {412 -- 418}, language = {en} } @misc{MirskyStozhkovaSzito, author = {Mirsky, Vladimir M. and Stozhkova, I. N. and Szito, T.}, title = {Photosensitized damage of bilayer lipid membrane in the presence of hematoporphyrin dimethylether}, series = {Journal of Photochemistry and Photobiology. B, Biology}, volume = {8}, journal = {Journal of Photochemistry and Photobiology. B, Biology}, number = {3}, issn = {1011-1344}, pages = {315 -- 324}, abstract = {The variations in electrical conductivity and surface tension of planar bilayer lipid membranes (BLMs) sensitized by a haematoporphyrin dimethylether (HpDME) on visible light irradiation are reported. The irradiation of BLMs immediately leads to a decrease in membrane surface tension. On irradiation the conductivity of BLMs remains constant for a certain period of time (induction time), followed by an increase, terminated by membrane breakage. The induction time is not dependent on stirring of the solution, the addition of azide or ferricyanide to the solution, the addition of antioxidant to the lipid or substitution of air for argon in the cell. The induction time decreases for repeated irradiations or for any new BLM formed in the same cell immediately after the previous membrane has been broken. The conductivity shift consists of reversible and irreversible components. These results suggest that the irradiation of BLMs sensitized by HpDME leads to an accumulation of photoproducts in the membrane which induce pore formation and to a decrease in BLM stability when the concentration of the photoproducts exceeds a critical level.}, language = {en} } @misc{PortnovMirskyMarkin, author = {Portnov, V. I. and Mirsky, Vladimir M. and Markin, Vladislav S.}, title = {Bacteriorhodopsin: current-voltage dependence}, series = {Bioelectrochemistry and Bioenergetics}, volume = {23}, journal = {Bioelectrochemistry and Bioenergetics}, number = {1}, issn = {0302-4598}, pages = {45 -- 63}, abstract = {Current-voltage dependences for different tentative bacteriorhodopsin models were studied in order to explain the linearity of this dependence observed in our previous experiments. It is proved that the best correspondence with experiment occurs when the passive proton transport path is assumed to contain many binding sites and the thickness of the widest barrier separating these sites is not more than 1 nm. One of the following two conditions is necessary: (1) electrostatic repulsion of protons in the channel is so strong that not more than one proton can be in the channel at a time; the potential energy of a proton in this channel decreases linearly towards the active site. (2) Electrostatic repulsion between protons in the channel is moderate, and the binding energy of a proton at all channel sites is equal. Under conditions of high channel occupation, single-file effects lead to non-linearity of the current-voltage characteristics if there is no electrostatic repulsion.}, language = {en} } @misc{StozhkovaMirsky, author = {Stozhkova, I. N. and Mirsky, Vladimir M.}, title = {Simulation of photoradiation therapy: photosensitized effect of hematoporphyrin dimethylether on planar bilayer lipid membrane}, series = {Bulletin of Experimental Biology and Medicine}, volume = {110}, journal = {Bulletin of Experimental Biology and Medicine}, number = {1}, issn = {0007-4888}, pages = {898 -- 900}, language = {en} } @misc{SokolovMirskyTothBoconadietal., author = {Sokolov, Valeri S. and Mirsky, Vladimir M. and Toth-Boconadi, R. and Markin, Vladislav S. and Kesthelyi, L.}, title = {Bacteriorhodopsin photocycle in decane}, series = {Biological membranes}, volume = {5}, journal = {Biological membranes}, issn = {0233-4755}, pages = {595 -- 599}, language = {en} } @misc{PortnovMirskyMarkin, author = {Portnov, V. I. and Mirsky, Vladimir M. and Markin, Vladislav S.}, title = {Current-voltage characteristic of bacteriorhodopsin}, series = {Biological membranes}, volume = {5}, journal = {Biological membranes}, issn = {0233-4755}, pages = {198 -- 216}, language = {en} } @inproceedings{MarkinMirskyChizmadzhev, author = {Markin, Vladislav S. and Mirsky, Vladimir M. and Chizmadzhev, Y. A.}, title = {Photoelectrical activity of bacteriorhodopsin in planar lipid bilayer}, series = {Receptors and Ion Channels, proceedings of the Symposium on Receptors and Ion Channels, Tashkent, USSR, Oct. 2 - 5, 1986}, booktitle = {Receptors and Ion Channels, proceedings of the Symposium on Receptors and Ion Channels, Tashkent, USSR, Oct. 2 - 5, 1986}, editor = {Ovchinnikov, Yurij A. and Hucho, F.}, publisher = {de Gruyter}, address = {Berlin [u.a.]}, isbn = {3-11-010346-X}, pages = {247 -- 254}, language = {en} } @misc{SokolovMirskyMarkinetal., author = {Sokolov, Valeri S. and Mirsky, Vladimir M. and Markin, Vladislav S. and Kazarinov, V. E.}, title = {Automatization of bioelectrochemical experiment}, series = {Soviet electrochemistry}, volume = {22}, journal = {Soviet electrochemistry}, pages = {959 -- 966}, language = {en} } @misc{MirskySokolovMarkinetal., author = {Mirsky, Vladimir M. and Sokolov, Valeri S. and Markin, Vladislav S. and Chekulaeva, L. N.}, title = {Bilayer lipid membrane formation from bacteriorhodopsin suspension in lipid solution}, series = {Biological membranes}, volume = {1}, journal = {Biological membranes}, issn = {0233-4755}, pages = {1143 -- 1150}, language = {en} } @misc{MirskySokolovMarkin, author = {Mirsky, Vladimir M. and Sokolov, Valeri S. and Markin, Vladislav S.}, title = {Reconstitution of bacteriorhodopsin in bilayer lipid membrane by monolayer method}, series = {Soviet electrochemistry}, volume = {20}, journal = {Soviet electrochemistry}, pages = {876}, language = {en} } @misc{MirskySokolovMelniketal., author = {Mirsky, Vladimir M. and Sokolov, Valeri S. and Melnik, E. I. and Diukova, T. V.}, title = {A study of incorporation of bacteriorhodopsin into bimolecular lipid membranes}, series = {Biophysics}, volume = {29}, journal = {Biophysics}, issn = {0006-3029}, pages = {250 -- 253}, language = {en} } @misc{MirskySokolov, author = {Mirsky, Vladimir M. and Sokolov, Valeri S.}, title = {Criteria of bacteriorhodopsin incorporation into bimolecular lipid membrane}, series = {Biophysics}, volume = {29}, journal = {Biophysics}, issn = {0006-3029}, pages = {246 -- 249}, language = {en} }