@misc{MirskyChernySokolovetal., author = {Mirsky, Vladimir M. and Cherny, Vladimir V. and Sokolov, Valeri S. and Markin, Vladislav S.}, title = {Electrostatic assay of phospholipase A activity: an application of the second harmonic method of monitoring membrane boundary potentials}, series = {Journal of Biochemical and Biophysical Methods}, volume = {21}, journal = {Journal of Biochemical and Biophysical Methods}, number = {4}, issn = {0165-022X}, pages = {277 -- 284}, abstract = {To evaluate phospholipase A activity a new assay is suggested. This assay is based on the recording of boundary potential changes of the planar bilayer lipid membrane during enzymatic hydrolysis of lipids. To register these changes, a second harmonic method is used. Sensitivity of the assay is about 0.0002 units/ml regardless of the impurities that may be present in the samples. One analysis takes about 5 min.}, language = {en} } @misc{ChernyMirskySokolovetal., author = {Cherny, Vladimir V. and Mirsky, Vladimir M. and Sokolov, Valeri S. and Markin, Vladislav S.}, title = {Determination of the phospholipase A activity}, series = {Biochemistry}, volume = {55}, journal = {Biochemistry}, number = {3}, pages = {445 -- 450}, language = {en} } @misc{MirskyChernySokolovetal., author = {Mirsky, Vladimir M. and Cherny, Vladimir V. and Sokolov, Valeri S. and Markin, Vladislav S.}, title = {Electrode for determination of the phospholipase activity based on the lipid membrane}, series = {Soviet electrochemistry}, volume = {25}, journal = {Soviet electrochemistry}, pages = {1336 -- 1340}, language = {en} } @misc{ChernyMirskySokolovetal., author = {Cherny, Vladimir V. and Mirsky, Vladimir M. and Sokolov, Valeri S. and Markin, Vladislav S.}, title = {BLM as an enzyme-sensitive electrode: determination of the phospholipase activity}, series = {Bioelectrochemistry and Bioenergetics}, volume = {21}, journal = {Bioelectrochemistry and Bioenergetics}, number = {3}, issn = {0302-4598}, pages = {373 -- 378}, 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{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{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{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} }