Author
Skorobogat'ko Ov
Bio: Skorobogat'ko Ov is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Ceruloplasmin & Electrode. The author has an hindex of 6, co-authored 10 publications receiving 776 citations.
Topics: Ceruloplasmin, Electrode, Electrode potential, Immunoassay, Blood serum
Papers
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665 citations
TL;DR: Two new enzymatic methods have been developed to quantify morphine and codeine simultaneously in a flow injection system (FIA) giving two signals without the requirement for a separation step, allowing discrimination between morphine andcodeine in less than 1 min after injection.
Abstract: Two new enzymatic methods have been developed to quantify morphine and codeine simultaneously in a flow injection system (FIA) The first enzyme sensor for morphine or codeine is based on immobilizing morphine dehydrogenase (MDH) and salicylate hydroxylase (SHL) on top of a Clark-type oxygen electrode Morphine or codeine oxidation by MDH leads to a consumption of oxygen by SHL via the production of NADPH This decreases the oxygen current of the Clark electrode Concentrations of codeine and morphine are detected between 2 and 1000 μM and between 5 and 1000 μM, respectively The second enzyme sensor for morphine is based on laccase (LACC) and PQQ-dependent glucose dehydrogenase (GDH) immobilized at a Clark oxygen electrode Morphine is oxidized by laccase under consumption of oxygen and regenerated by glucose dehydrogenase Since laccase cannot oxidize codeine, this sensor is selective for morphine Morphine is detected between 32 nM and 100 μM Both sensors can be operated simultaneously in one flow system (FIA) giving two signals without the requirement for a separation step This rapid and technically simple method allows discrimination between morphine and codeine in less than 1 min after injection The sampling rate for quantitative measurements is 20 h–1 The method has been applied to the quantitative analysis of codeine or morphine in drugs
77 citations
TL;DR: An electrochemical immunosensor based on a new detection principle was developed and laccase, which is able to catalyse the electroreduction of oxygen via the direct (mediatorless) mechanism was used as an enzyme label.
34 citations
TL;DR: Cp had an effect on rosetting only when lymphocytes were preincubated with it, suggesting that Cp binding to lymphocytes was responsible for these effects, and the decrease in all types of rosetting was dose-related.
Abstract: We investigated the effect of plasma ceruloplasmin (Cp) on the different types of lymphocyte rosetting, and phagocytosis of polystyrene particles and culture Candida albicans by peripheral blood neutrophils and monocytes. Lymphocytes, neutrophils, and monocytes were isolated from the blood of patients with elevated immuno-status (n = 9), healthy donors (n = 21), and patients with reduced immuno-status (n = 21). The ability of Cp to decrease the number of lymphocytes forming E- and EAC- rosettes and rosettes with auto-erythrocytes was shown for both patients and healthy donors. The maximal decrease of the number of E-rosettes (by 35%) and EAC-rosettes (by 57%) was shown for lymphocytes of the patients with elevated immuno-status. Cp had an effect on rosetting only when lymphocytes were preincubated with it, suggesting that Cp binding to lymphocytes was responsible for these effects. The decrease in all types of rosetting caused by Cp was dose-related, with a maximum effect at physiological concentration of...
13 citations
TL;DR: A new immunochemical reagent is suggested containing as an enzyme marker laccase obtained from the cultural liquid of basidial fungi Coriolus hirsutus, which is simpler than that employing antibody-peroxidase conjugates.
Abstract: A new immunochemical reagent is suggested containing as an enzyme marker laccase obtained from the cultural liquid of basidial fungi Coriolus hirsutus. The feasibility of immuno-laccase conjugates in different versions of immunoanalysis (sandwich, competitive and indirect enzyme immunoassay) was demonstrated. The assay based on antibodvlaccase conjugates is simpler than that employing antibody-peroxidase conjugates, since in the former case air oxygen is used as the second substrate of the enzymatic reaction.
11 citations
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TL;DR: This work has focused on more recent reports on the occurrence of laccase and its functions in physiological development and industrial utility and the reports of molecular weights, pH optima, and substrate specificity are extremely diverse.
1,309 citations
TL;DR: In this paper, a review of the applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area is presented, where they are also used as cleaning agents for certain water purification systems, as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics.
1,131 citations
TL;DR: The decolorization and detoxification potential of WRF can be harnessed thanks to emerging knowledge of the physiology of these organisms as well as of the biocatalysis and stability characteristics of their enzymes.
1,091 citations
TL;DR: Immobilization of oxidative enzymes on porous ceramic supports or resins did not adversely affect their stability and showed a good potential for degradation of environment persistent aromatics.
Abstract: A number of oxidative enzymes from bacteria, fungi and plants have been reported to play an important role in numerous waste treatment applications. Peroxidases and/or phenoloxidases can act on specific recalcitrant pollutants by precipitation or transforming to other products and permitting a better final treatment of the waste. Improvement in the useful life and thereby a reduction in treatment cost has been accomplished through enzyme immobilization. Horseradish peroxidase, lignin peroxidase and manganese peroxidase mineralize a variety of recalcitrant aromatic compounds. Immobilization of these enzymes on porous ceramic supports or resins did not adversely affect their stability and showed a good potential for degradation of environment persistent aromatics. Tyrosinase, which catalyzes the hydroxylation of phenols and dehydrogenation of o-diphenols, in an immobilized form exerted an excellent phenol removal. Laccase is capable of eliminating the phenols through polymerization process, however, the presence of mediator such as ABTS and HBT degraded phenol by oxidative process. Many applications with oxidative enzymes and plant materials in effluent as in soil remediation will be discussed.
894 citations
TL;DR: In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure–function relationships.
Abstract: Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.
807 citations