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226 records – page 1 of 23.

[A comparative analysis of the results of using different methods of helium-neon laser therapy in patients with stable stenocardia]

https://arctichealth.org/en/permalink/ahliterature11296
Source
Lik Sprava. 1996 Jan-Feb;(1-2):73-6
Publication Type
Article
Author
V M Iurlov
I H Kul'baba
Source
Lik Sprava. 1996 Jan-Feb;(1-2):73-6
Language
Ukrainian
Publication Type
Article
Keywords
Angina Pectoris - drug therapy - metabolism - radiotherapy
Antithrombin III - metabolism - radiation effects
Chronic Disease
Combined Modality Therapy
Comparative Study
English Abstract
Evaluation Studies
Humans
Lasers - therapeutic use
Liver - metabolism - radiation effects
Nitroglycerin - therapeutic use
Vasodilator Agents - therapeutic use
alpha 1-Antitrypsin - metabolism - radiation effects
alpha-Macroglobulins - metabolism - radiation effects
Abstract
Based on the findings from the examination of 133 patients with stable angina pectoris, it was shown that He-Ne laser therapy with the irradiation being applied to the liver projection area in combination with the prolonged-action nitrates is superior to similar application of irradiation to the precordial region and Head's zones or intravenous irradiation of blood. Revealed in the examination of the above patients was a reaction of antiproteolytic enzymes to He-Ne laser therapy, which appeared to be varying with methods of laser therapy. It is suggested that a reaction of the realization of the components of proteolysis might be involved in the realization of therapeutic effect of the He-Ne laser energy in patients with ischemic heart disease.
PubMed ID
9005112 View in PubMed
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[A comparative evaluation of the effect of different types of sapropel on dynamic liver function in intact rats and in the modelling of toxic hepatitis]

https://arctichealth.org/en/permalink/ahliterature56727
Source
Vopr Kurortol Fizioter Lech Fiz Kult. 1998 Mar-Apr;(2):37-8
Publication Type
Article
Author
D I Kuz'menko
G N Sidorenko
E F Levitskii
B I Laptev
E I Dzhuraeva
Source
Vopr Kurortol Fizioter Lech Fiz Kult. 1998 Mar-Apr;(2):37-8
Language
Russian
Publication Type
Article
Keywords
Animals
Benzopyrans - pharmacology - therapeutic use
Carbon Tetrachloride Poisoning - metabolism - rehabilitation
Comparative Study
Disease Models, Animal
English Abstract
Hepatitis, Toxic - metabolism - rehabilitation
Humic Substances - pharmacology - therapeutic use
Lipid Peroxidation - drug effects
Liver - drug effects - metabolism
Mud Therapy
Rats
Rats, Wistar
Reference Values
Seasons
Siberia
Abstract
A course of silicic sapropel applications compared to calcareous sapropel induced a reversible fall of total lipid concentration in blood serum of intact rats. Sapropels of different kinds and of the same kind but obtained from different depths of the same deposit varied by their ability to correct hepatic function in rats with toxic hepatitis. The highest benefit was registered in application of carbonate sapropels taken from the depth of 1.5-2.5 m.
PubMed ID
9643147 View in PubMed
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[A comparative study of activity of nucleic acid metabolism in human embryonic liver]

https://arctichealth.org/en/permalink/ahliterature66248
Source
Ukr Biokhim Zh. 1975 Nov-Dec;47(6):724-7
Publication Type
Article
Author
B H Borzenko
K O Drel'
Source
Ukr Biokhim Zh. 1975 Nov-Dec;47(6):724-7
Language
Ukrainian
Publication Type
Article
Keywords
Adult
Cell Nucleus - enzymology
DNA - metabolism
Deoxyribonucleases - metabolism
English Abstract
Female
Fetus - enzymology
Gestational Age
Humans
Liver - embryology - enzymology
Pregnancy
RNA - metabolism
Ribonucleases - metabolism
Thymidine Kinase - metabolism
Uridine Kinase - metabolism
Abstract
In nuclei of hepatocytes of human embryos from the 18th to 40th week of antenatal development the activity of synthesis enzymes lowers: thymidine kinase is 7 times at low, uridine kinase - 11 times as low. In parallel during the same period a decrease in the activity of nucleases drops: DNase - by 15 times, RNase - by 11 times. The activity of these enzymes in the liver of adult persons (22-35 years old) is similar to their activity in the liver of human embryo to the moment of birth.
PubMed ID
1202705 View in PubMed
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[Activities of the liver microsome reductases in adult and aged rats during stress]

https://arctichealth.org/en/permalink/ahliterature10009
Source
Vopr Med Khim. 2001 Nov-Dec;47(6):599-604
Publication Type
Article
Author
N P Rud'ko
V V Davydov
Author Affiliation
State Medical University, Mayakowsky av., 26, Zaporozhye, 69035, Ukraine.
Source
Vopr Med Khim. 2001 Nov-Dec;47(6):599-604
Language
Russian
Publication Type
Article
Keywords
Aging - metabolism
Animals
Comparative Study
English Abstract
Hydrogen Peroxide - pharmacology
Immobilization
Male
Microsomes, Liver - enzymology
Quinone Reductases - metabolism
Rats
Rats, Wistar
Sodium Dodecyl Sulfate - pharmacology
Stress, Psychological - enzymology
Urea - pharmacology
Abstract
The influence of 0.01% sodium dodecyl sulphate, 1.5 and 6.0 M urea and 0.03 M hydrogen peroxide to the NAD(P)H: 2,6 dichlorphenolindophenol reductase activity in livers of adult and old Wistar rats during immobilizing stress was interested. Obtained results indicate that the NADPH--dependent reductase is more resistant to modulating effect of sodium dodecyl sulphate, hydrogen peroxide and urea than NADH-dependent enzyme. The significant decrease of NADH: 2.6 dichlorphenolindophenol reductase sensitivity to the action of all studied modulators occurs in old rats. The similar changes appears in the adult rats liver during stress. The old rats immobilization is accompanied by a decrease of this enzyme activity and the reduction of the influence of all studied modulators to NADH: 2.6 dichlorphenolindophenol reductase as compared with adult ones. These changes in the activity and properties of microsomal NADH: 2,6 dichlorphenolindophenol reductase promote more pronounced decrease of the substrate hydroxylation in the liver of old rats during stress compared to adult ones.
PubMed ID
11925750 View in PubMed
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[Activity and induction of CYP2B, CYP2C, and CYP3A in tissues of cyclophosphane-sensitive and resistant neoplasms and the liver of neoplasm-carrying mice]

https://arctichealth.org/en/permalink/ahliterature18154
Source
Biomed Khim. 2003 Jan-Feb;49(1):27-34
Publication Type
Article
Author
A Iu Grishanov
V I Kaledin
T V Zueva
E K Nekhoroshkova
V P Nikolin
V V Liakhovich
Author Affiliation
Institute of Molecular Biology and Biophysics, Siberian Branch of Russian Academy of Medical Sciences, Timakova str., 2, Novosibirsk, 630117, Russia. agrish@cyber.ma.nsc.ru
Source
Biomed Khim. 2003 Jan-Feb;49(1):27-34
Language
Russian
Publication Type
Article
Keywords
Animals
Antineoplastic Agents - pharmacology - therapeutic use
Aryl Hydrocarbon Hydroxylases - biosynthesis - metabolism
Cyclophosphamide - pharmacology - therapeutic use
Cytochrome P-450 CYP2B1 - biosynthesis - metabolism
Cytochrome P-450 CYP3A
Cytochrome P-450 Enzyme System - biosynthesis - metabolism
Drug Resistance, Neoplasm
English Abstract
Enzyme Induction
Liver Neoplasms - drug therapy - enzymology
Lymphoma, Diffuse - drug therapy - enzymology
Male
Mice
Mice, Inbred CBA
Microsomes - enzymology
Neoplasm Transplantation
Oxidoreductases, N-Demethylating - biosynthesis - metabolism
Abstract
The activities of three cytochrome P450 families involved in metabolic transformation of cyclophosphamide (CP) (CYP2B and CYP2C responsible for metabolic activation of CP and CYP3A responsible for inactivation of CP) have been investigated in lymphosarcoma and liver microsomes of tumor-bearing CBA mice. Two strains of mouse lymphosarcoma distinguished by their sensitivity to cytostatic action of CP were used in this study for implantation in mice femur muscle. There was certain relationship between CP resistance of lymphosarcoma and tumor P450s activity. CYP2B, CYP2C and CYP3A activities in the CP sensitive tumor were comparable to those in liver, and CYP2B, CYP2C were induced by phenobarbital and dexamethasone. CYP2B and CYP2C in the CP resistant tumor were inactive and only slightly induced by dexamethasone. CYP3A activity was lower than in LS tumor and unchanged during drug treatment. Implantation of LS and RLS tumor in mice caused different effects on P450 activities. LS insignificantly influenced liver CYP2B, CYP2C and CYP3A activities and their inducibility by phenobarbital and dexamethasone was similar to that obtained in liver of mice without tumor. At the same time, CYP2B and CYP2C activity in liver of RLS-bearing mice were essentially reduced, the activity CYP3A remained unchanged, and inducibility of CYP2B, CYP2C and CYP3A by phenobarbital and dexamethasone was similar to that in liver of mice without tumor. These results prove the role of cytochromes P450 activating CP in formation drug resistant phenotype of mice lymphosarcoma and suggest possibility of overcoming of this resistance using cytochrome P450 inducers.
PubMed ID
14569871 View in PubMed
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[Activity of carbohydratephosphate metabolism enzymes in liver slices after freezing and thawing]

https://arctichealth.org/en/permalink/ahliterature13160
Source
Ukr Biokhim Zh. 1977 May-Jun;49(3):10-5
Publication Type
Article
Author
V I Lugovii
L I Zolochevs'ka
A M Dziuba
Source
Ukr Biokhim Zh. 1977 May-Jun;49(3):10-5
Language
Ukrainian
Publication Type
Article
Keywords
Animals
Drug Stability
English Abstract
Freezing
Glucosephosphate Dehydrogenase - metabolism
Hexokinase - metabolism
L-Lactate Dehydrogenase - metabolism
Liver - drug effects - enzymology
Phosphorylases - metabolism
Polyethylene Glycols - pharmacology
Rats
Subcellular Fractions - enzymology
Abstract
Activity of hexokinase, phosphorylase, glucoso-6-phosphate dehydrogenase lactate-dehydrogenase was studied in liver slices, homogenate and supernatant fraction after freezing at a rate of 1 degree/min down to -30 degrees C. The enzyme activity in homogenate and supernatant fraction does not change after freezing. A significant reduction in the activity of most enzymes that is followed by an increase in their activity in the freezing medium was observed in the experiments. Cryoprotectant polyethylene glycol, mol. wt. 300 and 1,000 (PEG-300 and PEG-1,000), partially prevents the observed changes in the enzyme activity; PEG-1,000 is more effective than PEG-300. Experimental results show that the main reason for the reduction of the enzyme activity observed after freezing the tissue slices is a decrease in the volume of intracellular enzyme proteins due to their leakage from the injured cellular elements into the exocellular medium.
PubMed ID
888219 View in PubMed
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[Activity of cytoplasmic proteinases from rat liver in Heren's carcinoma during tumor growth and treatment with medicinal herbs]

https://arctichealth.org/en/permalink/ahliterature20009
Source
Ukr Biokhim Zh. 2000 May-Jun;72(3):91-4
Publication Type
Article
Author
M M Marchenko
H P Kopyl'chuk
O V Hrygor'ieva
Author Affiliation
Yu. Fedkovich Chernivtsi State University, Ukraine.
Source
Ukr Biokhim Zh. 2000 May-Jun;72(3):91-4
Language
Ukrainian
Publication Type
Article
Keywords
Animals
Cytoplasm - enzymology
English Abstract
Hydrolysis
Liver - enzymology - pathology
Liver Neoplasms - enzymology
Organ Size - drug effects
Plant Extracts - pharmacology
Plants, Medicinal - chemistry
Rats
Abstract
The dynamics of the acid and neutral proteinases general enzymes activity change in the hepatocytes postnuclear fraction in the rats suffering from the Heren's carcinoma was investigated. It was determined that in the tumor development of the enzyme activity level of both the acid and neutral proteinases increased 2,6-fold. The natural preparation of the herbs (Calendula officinalis L., Echinacea purpurea L., Scorzonera humilis L., Aconitum moldavicum Hacq.) normalizes both the activity of the investigated enzymes and coefficients of the liver weights of the sick animals. The chemical medicinal preparation 5,6-benzcumarine-5-uracil normalizes the activity of the neutral cytoplasmatic proteinases and reduces the level of the proteolytic activity of the acid enzymes in comparison with the control group of the animals as well as increases of the liver weight coefficients.
PubMed ID
11200483 View in PubMed
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[Activity of glutathione-S-transferase in the blood plasma, liver and crystalline lens tissues as affected by low doses of ionizing radiation and polychromatic light]

https://arctichealth.org/en/permalink/ahliterature51029
Source
Ukr Biokhim Zh. 1997 May-Jun;69(3):54-9
Publication Type
Article
Author
N F Leus
S G Kolomiichuk
V B Lishchenko
Author Affiliation
V.P. Filatov Institute of Eye Diseases and Tissue Therapy, Academy of Medical Sciences of Ukraine, Odessa.
Source
Ukr Biokhim Zh. 1997 May-Jun;69(3):54-9
Language
Russian
Publication Type
Article
Keywords
Animals
Dose-Response Relationship, Radiation
English Abstract
Glutathione Transferase - blood - metabolism - radiation effects
Lens, Crystalline - enzymology - radiation effects
Light
Liver - enzymology - radiation effects
Male
Rabbits
Abstract
The developmental dynamics of pathologic changes in the lenses and activity of glutathione-S-transferase in the blood plasma, liver and lens tissues of rabbits under chronic influence (2 months) of small doses of X-ray radiation (total dose 2 Gy) and polychromatic light have been researched. It was shown, that polychromatic light and X-ray irradiation of rabbits significantly affected the lens nativity and increased the developmental frequency and the intensity of lens opacities. It was determined, that activity of glutathione-S-transferase in blood plasma increased for 1 month after the beginning of X-ray effects. The same effect on the enzymatic activity was shown by the summary influence of polychromatic light and X-ray irradiation. Glutathione-S-transferase activity decreased during 2 months as compared with the initial values, before irradiation of the animals. The enzymatic activity was increased in rabbit-liver cytoplasm by X-ray irradiation in 2 months. A decrease of glutathione-S-transferase activity in the liver, cortex and lens nucleus was determined under the influence of both X-ray radiation and polychromatic light.
PubMed ID
9505362 View in PubMed
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[Activity of organ specific enzymes in animals with liver damage following administration of antihepatocytotoxic serum]

https://arctichealth.org/en/permalink/ahliterature57079
Source
Fiziol Zh. 1976 Sep-Oct;22(5):611-5
Publication Type
Article

[Adenylate system of rat liver tissue during chemical carcinogenesis]

https://arctichealth.org/en/permalink/ahliterature27769
Source
Ukr Biokhim Zh. 1977 Jan-Feb;49(1):87-90
Publication Type
Article
Author
L I Loevskaia
Source
Ukr Biokhim Zh. 1977 Jan-Feb;49(1):87-90
Language
Ukrainian
Publication Type
Article
Keywords
Adenine Nucleotides - metabolism
Adenosinetriphosphatase - metabolism
Adenylate Kinase - metabolism
Animals
Diethylnitrosamine
English Abstract
Liver - enzymology - metabolism
Male
Neoplasms, Experimental - chemically induced - enzymology - metabolism
Phosphotransferases - metabolism
Rats
p-Dimethylaminoazobenzene
Abstract
The ratio of adenylic nucleotides, activity of adenylatekinase and ATPase were studied in the liver subcellular fractions and in tumours of rats with cancerogenesis induced by diethylnitrozamine and p-dimethylaminoazobenzene. The adenylatekinase activity increases in the liver hyaloplasm of rats with tumours and in the tissue of the tumours themselves, the activity of ATPase is unchanged. An increase in the adenylatekinase activity in hyaloplasm is accompanied by a decrease in the level of ATP with the absence of changes in ADP and AMP, that results in a drop "of the adenylate energy charge" value (Atkinson reflecting the balance of adenyl nucleotides in a cell.
PubMed ID
194377 View in PubMed
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226 records – page 1 of 23.