[Design of experimental approaches on the base of standard proteins for testing blood biopreparations and immunoperoxidase conjugates specific to human and animal immunoglobulines G].

Using standard forms of immunoglobulin (Ig) G and albumin, we have studied electrophoretic and chromatographic profiles of samples of pharmaceutical blood biopreparation batches. The usability of standard proteins was also demonstrated by testing analytical characteristics of immunoperoxidase conjugates specific to human and animal IgG (anti-IgG IPC). In particular, we suggest an additional estimation of analytical characteristics of anti-IgG IPC by the enzyme reaction kinetics with the standard dilution which is calculated by the direct enzyme-liked immunoassay on the homologous IgG-antigen.

Potentiometric biosensors for cholinesterase inhibitor analysis based on mediatorless bioelectrocatalysis.

A potentiometric method for cholinesterase inhibitor analysis based on mediatorless bioelectrocatalysis has been developed. The method includes coimmobilization of three enzymes, butyrylcholinesterase, choline oxidase and peroxidase, on composite carbon electrodes. Catalytic hydrolysis of butyrylcholine and subsequent catalytic oxidation of choline result in the formation of hydrogen peroxide leads to a shift in the electrode potential. The detection limit for trichlorfon analysis is 2 x 10(-13) M. Electrodes remain stable for at least 4 weeks when stored at 277 K.

New catalytic properties of monoamine oxidase immobilized in Langmuir-blodgett films with amphiphilic polyelectrolytes.

Langmuir-Blodgett (LB) films of monoamine oxidase (MAO) have been formed on the surface f a polypropylene membrane using amphiphilic polyelectrolytes. The enzyme activity of such protein-polyelectrolyte films was measured by a Clark electrodes. It was shown that in LB films thus formed the use of amphiphilc polyelectrolytes, MAO activity was higher than in polyelectrolyte-free LB films. Immobilization of MAO with branched polyethylenimine modified on 12% by laurylchain led to pronounced changes in its catalytic properties. The dependence of the enzyme's kinetic parameters on amphiphilic polyelectrolyte structures was discussed. (c) 1994 John Wiley & Sons, Inc.