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1.
Ukr Biochem J ; 88(2): 66-72, 2016.
Article in English | MEDLINE | ID: mdl-29227606

ABSTRACT

The rate of superoxide anion radical, hydroxyl radical and hydrogen peroxide generation, the level of oxidative modification of mitochondrial proteins in the liver of rats with toxic hepatitis was investigated on the background of alimentary protein deficiency. We did not find significant increases of the intensity of free radical processes in liver mitochondria of rats maintained on the protein-deficient ration. The most significant intensification of free radical processes in liver mitochondria is observed under the conditions of toxic hepatitis, induced on the background of alimentary protein deprivation. Under these conditions the aggravation of all studied forms of reactive oxygen species generation was observed in liver mitochondria. The generation rates were increased as follows: O2 ­ by 1.7 times, Н2О2 ­ by 1.5 times, •ОН ­ practically double on the background of accumulation of oxidized mitochondria-derived proteins. The established changes in thiol groups' redox status of respiratory chain proteins insoluble in 0.05 M sodium-phosphate buffer (pH 11.5), and changes of their carbonyl derivatives content may be considered as one of the regulatory factors of mitochondrial energy-generating function.


Subject(s)
Chemical and Drug Induced Liver Injury/metabolism , Hydrogen Peroxide/metabolism , Hydroxyl Radical/metabolism , Mitochondria, Liver/metabolism , Protein Deficiency/metabolism , Superoxides/metabolism , Acetaminophen/toxicity , Animals , Animals, Outbred Strains , Chemical and Drug Induced Liver Injury/complications , Chemical and Drug Induced Liver Injury/pathology , Diet, Protein-Restricted/adverse effects , Hydrogen Peroxide/agonists , Hydroxyl Radical/agonists , Liver/drug effects , Liver/metabolism , Liver/pathology , Mitochondria, Liver/drug effects , Oxidation-Reduction , Oxidative Stress , Protein Carbonylation , Protein Deficiency/complications , Protein Deficiency/etiology , Protein Deficiency/pathology , Rats , Superoxides/agonists
2.
Ukr Biochem J ; 87(1): 121-6, 2015.
Article in Ukrainian | MEDLINE | ID: mdl-26036138

ABSTRACT

The ratio between the redox forms of the nicotinamide coenzymes and key enzymatic activity of the I and II respiratory chain complexes in the liver cells mitochondria of rats with acetaminophen-induced hepatitis under the conditions of alimentary deprivation of protein was studied. It was estimated, that under the conditions of acute acetaminophen-induced hepatitis of rats kept on a low-protein diet during 4 weeks a significant decrease of the NADH:ubiquinone reductase and succinate dehydrogenase activity with simultaneous increase of the ratio between redox forms of the nicotinamide coenzymes (NAD+/NADH) is observed compared to the same indices in the liver cells of animals with experimental hepatitis kept on the ration balanced by all nutrients. Results of research may become basic ones for the biochemical rationale for the approaches directed to the correction and elimination of the consequences of energy exchange in the toxic hepatitis, induced on the background of protein deficiency.


Subject(s)
Acetaminophen/toxicity , Chemical and Drug Induced Liver Injury/enzymology , Electron Transport Complex I/metabolism , Mitochondria, Liver/enzymology , Protein Deficiency/enzymology , Succinate Dehydrogenase/metabolism , Animals , Animals, Outbred Strains , Chemical and Drug Induced Liver Injury/pathology , Diet, Protein-Restricted/adverse effects , Male , Mitochondria, Liver/pathology , NAD/metabolism , Oxidation-Reduction , Protein Deficiency/etiology , Protein Deficiency/pathology , Rats
3.
Ukr Biokhim Zh (1999) ; 80(4): 114-9, 2008.
Article in Ukrainian | MEDLINE | ID: mdl-19140457

ABSTRACT

The work is devoted to investigation of the influence of low doses of preliminary radiation on the fraction content, and oxidizing modification of mitochondrial proteins, unsolvable in 0.05 M sodium-phosphate buffer (11,5), and mtDNA fragmentation. That low-dose irradiation influence mostly manifests itself on the initial stages of tumor growth. It was established that tumor development is accompanied with the changes of mitochondrial proteins fraction content. These changes occured on the intensive oxidizing modification background of the proteins under study and mtDNA fragmentation.


Subject(s)
DNA, Mitochondrial/metabolism , Mitochondria/radiation effects , Mitochondrial Proteins/metabolism , Neoplasms, Experimental/metabolism , Animals , DNA Fragmentation/radiation effects , Dose-Response Relationship, Radiation , Hydrogen-Ion Concentration , Mitochondria/metabolism , Mitochondrial Proteins/chemistry , Molecular Weight , Radiation Dosage , Radiation, Ionizing , Rats , Solubility
4.
Bull Exp Biol Med ; 144(4): 520-2, 2007 Oct.
Article in English | MEDLINE | ID: mdl-18642702

ABSTRACT

We demonstrated specific features of oxidative damage to mitochondrial translation products in animals were revealed after fractionated X-ray exposure in low doses. Differences were found in carbonylation and oxidation of SH groups in irradiated rats and irradiated tumor-bearing animals. Our results indicate that preliminary fractionated X-ray exposure determines oxidative damage to these mitochondrial proteins only at the initial stage of the study, while in the follow-up period major role is played the by tumor development.


Subject(s)
Mitochondria/radiation effects , Mitochondrial Proteins/biosynthesis , Protein Biosynthesis/radiation effects , X-Rays , Animals , Carcinoma, Transitional Cell/metabolism , Carcinoma, Transitional Cell/pathology , Male , Mitochondria/metabolism , Oxidation-Reduction/radiation effects , Protein Carbonylation/radiation effects , Rats , Urinary Bladder Neoplasms/metabolism , Urinary Bladder Neoplasms/pathology
5.
Lab Delo ; (4): 21-3, 1991.
Article in Russian | MEDLINE | ID: mdl-1715423

ABSTRACT

A diagnostic agent for enzyme immunoassay of ceruloplasmin has been developed. The method is highly sensitive and specific. The minimal detectable amount of ceruloplasmin is 25 ng/ml, variance coefficients with 1 lot being 2.6-7.3 percent and 4.2-10.8 percent within 3 lots. Blood serum ceruloplasmin concentration in health has made up 0.9 to 1.3 mg/ml. Ceruloplasmin levels were regularly shifted in Wilson's disease, cerebral lymphomas, sepsis, injuries, liver cirrhosis and other diseases.


Subject(s)
Ceruloplasmin/analysis , Immunoenzyme Techniques , Female , Humans , Indicators and Reagents , Male , Reference Values
6.
Lab Delo ; (12): 55-9, 1990.
Article in Russian | MEDLINE | ID: mdl-1710697

ABSTRACT

Changes in plasma ceruloplasmin levels were studied by enzyme immunoassay in 81 patients with the acute hepatorenal insufficiency syndrome (AHIS). Changed plasma ceruloplasmin concentration was detected in the first days of the disease, this change depending on AHIS severity and unrelated to the disease cause. A lowering of plasma ceruloplasmin level below 0.75 mg/ml is considered to be a poor prognostic sign. Measurement of plasma ceruloplasmin is a test available for clinical laboratories, it is highly sensitive, accurate, and reproducible.


Subject(s)
Ceruloplasmin/analysis , Hepatorenal Syndrome/blood , Humans , Immunoenzyme Techniques
9.
Article in Russian | MEDLINE | ID: mdl-3055765

ABSTRACT

The data on the comparison of the quality of polystyrene plates manufactured in the USSR with those manufactured by a number of foreign producers are presented. These data indicate that the capacity of antibodies adsorbed on a polystyrene plate for the sorption of antigens depend on the properties of the polymer surface and vary for different plates.


Subject(s)
Immunoenzyme Techniques/instrumentation , Polystyrenes/analysis , Immunosorbents
11.
Article in Russian | MEDLINE | ID: mdl-3300700

ABSTRACT

Clinical trials of immunoenzyme test-systems for the quantitative determination of fibronectin, fibrinogen, fibrin/fibrinogen degradation products and myoglobin have been performed on serum and plasma samples obtained from patients and healthy donors. The tests were informative and possessed diagnostic value in the following conditions: fibronectin--in pyogenic septic complications of newborns, burn infections; fibrinogen and fibrin/fibrinogen products--in thrombosis, myocardial infarction and disseminated intravascular coagulation syndrome; myoglobin--in myocardial infarction.


Subject(s)
Diagnosis , Fibrin Fibrinogen Degradation Products/analysis , Fibrinogen/analysis , Fibronectins/blood , Myoglobin/blood , Adult , Evaluation Studies as Topic , Humans , Immunoenzyme Techniques/instrumentation , Infant, Newborn , Reagent Kits, Diagnostic
12.
Vopr Med Khim ; 32(6): 123-6, 1986.
Article in Russian | MEDLINE | ID: mdl-3544487

ABSTRACT

Quantitative immunoenzyme assay of fibronectin in blood plasma is developed. Isolation and purification of fibronectin from human blood plasma, harvesting of specific antibodies to fibronectin, production of the antibodies and peroxidase conjugates and step-by-step procedure of the immunoenzyme assay in a "sandwich" modification are described. The assay was applied for diagnostics of several infectious and somatic diseases.


Subject(s)
Fibronectins/analysis , Humans , Immunoenzyme Techniques
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