Výsledky vyhledávání - "Z S, Mkrtchian"

[Effect of low-intensity 900 MHz frequency electromagnetic radiation on rat liver and blood serum enzyme activities]

Autor: L S, Nersesova, M S, Petrosian, M G, Gazariants, Z S, Mkrtchian, G O, Meliksetian, L G, Pogosian, Zh I, Akopian

Publikováno v: Radiatsionnaia biologiia, radioecologiia. 54(5)

The comparative analysis of the rat liver and blood serum creatine kinase, alanine aminotransferase, aspartate aminotransferase, alkaline phosphatase and purine nucleoside phosphorylase post-radiation activity levels after a total two-hour long singl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b45044b735315e2b618c57f1f6c7e963
https://pubmed.ncbi.nlm.nih.gov/25775844

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[Influence of ionizing radiation on enzymatic activity and state of nucleus-nucleolar apparatus in rat hepatocytes]

Autor: L S, Nersesova, M G, Gazariants, Z S, Mkrtchian, G O, Meliksetian, L G, Pogosian, S A, Pogosian, L L, Pogosian, E M, Karalova, A S, Avetisian, l O, Abroian, Z A, Karalian, Zh I, Akopian

Publikováno v: Radiatsionnaia biologiia, radioecologiia. 53(1)

The effects of a single exposure of rats to the whole-body roentgen irradiation at the doses of 3.5 Gy and 4.5 Gy on the activity of creatine kinase, purine nucleoside phosphorylase, alanine aminotransferase, aspartate aminotransferase, as well as on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::24bf0c2cf133f34d7dc0a0f781a0b8bf
https://pubmed.ncbi.nlm.nih.gov/23700835

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[Purine nucleoside phosphorylase inhibitors and their clinical significance]

Autor: L G, Pogosian, L S, Nersesova, M G, Gazariants, Z S, Mkrtchian, G O, Meliksetian, Zh I, Akopian

Publikováno v: Ukrains'kyi biokhimichnyi zhurnal (1999 ). 80(5)

PNP catalyzes a reversible phosphorolysis of purine deoxy- and ribonucleosides with formation of (d)Rib-1-P and appropriate bases. PNP plays a leading role in the cell metabolism of nucleosides and nucleotides, as well as in maintaining the immune st

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::020b1cf8ab59e3f099794956c7f82280
https://pubmed.ncbi.nlm.nih.gov/19248622

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[Role of individual phospholipids in the functional activity of human myocardial creatine kinase]

Autor: G O, Meliksetian, I M, Zarafian, Z S, Mkrtchian, Zh I, Akopian, K G, Karagezian

Publikováno v: Voprosy meditsinskoi khimii. 37(5)

Regulating effect of individual phospholipids on the activity of creatine kinase MM from human myocardium was studied. Cardiolipin, phosphatidic acid, phosphatidyl serine and phosphatidyl choline (dipalmitoyl) stimulated the enzymatic activity, while

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::414a9f214a9912a5cc4bc78167bb4494
https://pubmed.ncbi.nlm.nih.gov/1759405

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[Purification and various properties of creatine kinase MM isoenzyme from the human heart muscle]

Autor: G O, Meliksetian, Z S, Mkrtchian, Zh I, Akopian

Publikováno v: Voprosy meditsinskoi khimii. 33(2)

Homogeneous preparation of creatine kinase MM isoenzyme was isolated from human heart muscle using affinity chromatography on Sepharose containing immobilized Cibachron blue F3G-A. The enzyme was active at a wide range of pH 5.0-8.0 exhibiting maxima

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2bc68070f04b23d9639ff8283b58cf72
https://pubmed.ncbi.nlm.nih.gov/3604132

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[Structural-functional non-identity of subunits of creatine kinase from rabbit skeletal muscle]

Autor: G A, Nevinskiĭ, V N, Ankilova, O I, Lavrik, Z S, Mkrtchian, L S, Nersesova

Publikováno v: Biokhimiia (Moscow, Russia). 48(2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::035269a535b16fae37deefd0b22a86e3
https://pubmed.ncbi.nlm.nih.gov/6838931

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[Interaction of rabbit muscle creatine kinase with a reactive ATP derivative-ATP gamma-4(N-2-chloroethyl-N-methyl-amino)-benzylamidate]

Autor: Z S, Mkrtchian, L S, Nersesova, Zh I, Akopian, G T, Babkina, V N, Buneva

Publikováno v: Biokhimiia (Moscow, Russia). 45(5)

The interaction of AGP gamma-4(N-2-chloroethyl-N-methyl-amino)-benzylamidate with rabbit muscle creatine kinase was studied. ATP gamma-4-(N-2-hydroxyethyl-N-methyl-amino)-benzylamidate acts as competitive inhibitor of creatine kinase. The Km value fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3bbaac5a97b414402dff0ae266fa28f5
https://pubmed.ncbi.nlm.nih.gov/7378502

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[Creatine kinase from rabbit skeletal muscles: formation of O-acyltyrosine as a result of the activation of the carboxylic group of the enzyme active site by affinity reagents, nucleotide imidazolides]

Autor: G A, Nevinskiĭ, O I, Lavrik, M G, Gazariants, Z S, Mkrtchian, Zh I, Akopian

Publikováno v: Bioorganicheskaia khimiia. 13(4)

Creatine kinase from skeletal muscle (EC 2.7.3.2) was inactivated by means of imidazolides of AMP, ADP, ATP. Rates of the inactivation of the enzyme's M- and M'-subunits differ 50-100 fold and decrease in the presence of ADP and ATP. Differential spe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a42f1675a154ab03591ec5982603564c
https://pubmed.ncbi.nlm.nih.gov/3606672

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[Affinity modification of creatine kinase from rabbit skeletal muscle by 2',3'-dialdehyde derivatives of ADP and ATP]

Autor: G A, Nevinskiĭ, M G, Gazariants, Z S, Mkrtchian

Publikováno v: Bioorganicheskaia khimiia. 9(4)

Periodate-oxidized ADP and ATP (oADP and oATP) are substrates and affinity reagents for creatine kinase from rabbit skeletal muscle. oADP and oATP modified a lysine epsilon-amino group in the nucleotide-binding site of the enzyme. Complete inactivati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::78bf2d980a52cda0ed368aa32088dbe5
https://pubmed.ncbi.nlm.nih.gov/6679775

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