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Amino acid composition of epilithic biofilm and benthic animals in a large Siberian river / A. A. Kolmakova [et al.] // Freshwater Biology. - 2013. - Vol. 58, Is. 10. - P2180-2195, DOI 10.1111/fwb.12200 . - ISSN 0046-5070
Кл.слова (ненормированные):
Amino acids -- Epilithic microalgae and cyanobacteria -- Nutritive quality -- River ecosystem -- Zoobenthos
Аннотация: We studied amino acid (AA) composition of epilithic biofilms and zoobenthos near the shore at a middle section of the Yenisei River (Siberia, Russia). We hypothesised that there was an imbalance between the composition and content of amino acids in the biofilm and its consumers, the zoobenthos, as well as between those in the zoobenthos and fish. Based on monthly sampling from 2007 to 2010, there was seasonal variation in AA profiles in the epilithic biofilms, probably caused by the succession of microalgal and cyanobacterial species. Overall, there was an imbalance in the percentage of the essential amino acids (lysine and histidine) between benthic animals and their food (the epilithic biofilm), which suggests that benthic animals may be limited by food quality. Moreover, the zoobenthos had a significantly higher content of AA, relative to carbon, than the biofilm. Based on sampling in 2012, there was an imbalance between the AA profiles of zoobenthos and that of their main consumer, the Siberian grayling (Thymallus arcticus), particularly in the percentages of two essential amino acids, lysine and leucine. In terms of overall content of essential amino acids, the nutritional value to fish of gammarids, which have recently invaded the river, was significantly lower than that of indigenous taxa, trichopteran and chironomid larvae. В© 2013 John Wiley & Sons Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Science, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kolmakova, A.A.; Gladyshev, M.I.; Kalachova, G.S.; Kravchuk, E.S.; Ivanova, E.A.; Sushchik, N.N.

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Dynamics of amino acid composition of the medium during culture of isolated liver and kidneys by the controlled perfusion method / V. A. Barashkov [et al.] // Bulletin of Experimental Biology and Medicine. - 1976. - Vol. 80, Is. 11. - P1305-1307 . - ISSN 0007-4888
Кл.слова (ненормированные):
amino acid -- dog -- in vitro study -- kidney perfusion -- liver perfusion -- theoretical study
Аннотация: The dynamics of the amino acid composition of the medium was investigated during perfusion of the dog liver and kidney for 6 h with a mixture of autogenous plasma and medium No.199 in the ratio of 2:3. During culture of the kidney for 6 h the histidine concentration in the medium increased by 2.2 times compared with initially, the concentration of glutamic acid by 1.7 times, and of alanine and lysine by 1.6 times, whereas the concentrations of arginine, serine, and aspartic acid fell by 3.3 times and those of glutamine with threonine by 2.5 times. During perfusion of the liver the concentration of glutamic acid rose by 2.9 times, of alanine by 2.3 times, cystine by 2.0 times, and glycine by 1.5 times. The concentration of tyrosine fell by half, and that of phenylalanine and serine by 1.4 times. The arginine concentration fell so quickly during perfusion of the liver that by the second hour after the beginning of perfusion no arginine could be found in the medium. The method of amino acid analysis during organ culture as described can be used as a method of developing and correcting culture media.

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Держатели документа:
Siberian Div., Dept. Biophys., L.V. Kirenskii Inst. Phys., Acad. Sci. USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Barashkov, V.A.; Gitel'zon, I.I.; Nefedov, V.P.; Trubachev, I.N.

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Dynamics of amino acid composition of the medium in isolated organ culture by the controlled perfusion method / V. A. Barashkov [et al.] // Bulletin of Experimental Biology and Medicine. - 1975. - Vol. 80, Is. 7. - P759-761 . - ISSN 0007-4888
Кл.слова (ненормированные):
amino acid -- tissue culture medium -- dog -- in vitro study -- organ culture -- organ perfusion -- theoretical study
Аннотация: The dynamics of the amino acid composition of the perfusion fluid was investigated during adequate perfusion of isolated dog organs (the thorax and a complex consisting of the thoracic organs, kidneys, and liver). The concentration of amino acids such as histidine, lysine, and alanine in the perfusion fluid 6 h after the beginning of perfusion of the organ complex was higher, whereas that of arginine, serine, aspartic acid, threonine with glutamine, isoleucine, proline, leucine, and valine was much lower than initially. In experiments on the isolated thorax the dynamics of the amino acid composition of the medium was studied during perfusion for 4 h. The concentration of alanine, lysine, and histidine in the medium increased, whereas those of serine, aspartic acid, isoleucine, tyrosine, and phenylalanine decreased.

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Держатели документа:
Siberian Div., Dept. Biophys., L.V. Kirenskii Inst. Phys., Acad. Sci. USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Barashkov, V.A.; Gitel'zon, I.I.; Nefedov, V.P.; Trubachev, I.N.

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Luminescence of Ca(2+)-activated photoprotein obelin initiated by NaOCl and MnCl2. / E. S. Vysotski [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P301-305 . - ISSN 0884-3996
Кл.слова (ненормированные):
calcium -- chloride -- hypochlorite sodium -- manganese chloride -- manganese derivative -- obelin -- photoprotein -- article -- chemistry -- drug effect -- kinetics -- luminescence -- metabolism -- Calcium -- Chlorides -- Kinetics -- Luminescence -- Luminescent Proteins -- Manganese Compounds -- Sodium Hypochlorite
Аннотация: The luminescence of obelin is initiated by NaOCl in a reaction mixture containing no calcium. The addition of Mn2+ enhances the light emission > 300-fold. Sodium azide and histidine, as singlet oxygen quenchers, inhibit NaOCl-activated obelin luminescence in the presence or absence of Mn2+. This suggests that the addition of NaOCl to the mixture causes singlet oxygen formation (stimulated by Mn2+ ions), and singlet oxygen initiates the light-emitting reaction.

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Держатели документа:
Laboratory of Photobiology, Russian Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Trofimov, K.P.; Bondar', V.S.; Gitelson, J.I.

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Ni2+-zeolite/ferrosphere and Ni2+-silica/ferrosphere beads for magnetic affinity separation of histidine-tagged proteins / T. A. Vereshchagina [et al.] // Dalton Trans. - 2016. - Vol. 45, Is. 4. - P1582-1592, DOI 10.1039/c5dt03827h . - ISSN 1477-9226
Кл.слова (ненормированные):
Alkalinity -- Amino acids -- Chemical modification -- Fly ash -- Hydrothermal synthesis -- Ion exchange -- Magnetic separation -- Magnetism -- Proteins -- Silica -- Zeolites -- Conventional methods -- Core shell structure -- Green fluorescent protein -- Histidine-tagged proteins -- Hydrothermal treatments -- Magnetic affinity -- Mesoporous Silica -- Sorption capacities -- Nickel
Аннотация: Magnetic Ni2+-zeolite/ferrosphere and Ni2+-silica/ferrosphere beads (Ni-ferrosphere beads - NFB) of a core-shell structure were synthesized starting from coal fly ash ferrospheres having diameters in the range of 0.063-0.050 mm. The strategy of NFB fabrication is an oriented chemical modification of the outer surface preserving the magnetic core of parent beads with the formation of micro-mesoporous coverings. Two routes of ferrosphere modification were realized, such as (i) hydrothermal treatment in an alkaline medium resulting in a NaP zeolite layer and (ii) synthesis of micro-mesoporous silica on the glass surface using conventional methods. Immobilization of Ni2+ ions in the siliceous porous shell of the magnetic beads was carried out via (i) the ion exchange of Na+ for Ni2+ in the zeolite layer or (ii) deposition of NiO clusters in the zeolite and silica pores. The final NFB were tested for affinity in magnetic separation of the histidine-tagged green fluorescent protein (GFP) directly from a cell lysate. Results pointed to the high affinity of the magnetic beads towards the protein in the presence of 10 mM EDTA. The sorption capacity of the ferrosphere-based Ni-beads with respect to GFP was in the range 1.5-5.7 mg cm-3. © The Royal Society of Chemistry.

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Держатели документа:
Institute of Chemistry and Chemical Technology SB RAS, 50/24 Akademgorodok, Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, 50/50 Akademgorodok, Krasnoyarsk, Russian Federation
Siberian Federal University, 79 Svobodnyi Avenue, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Vereshchagina, T. A.; Fedorchak, M. A.; Sharonova, O. M.; Fomenko, E. V.; Shishkina, N. N.; Zhizhaev, A. M.; Kudryavtsev, A. N.; Frank, L. A.; Anshits, A. G.

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The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins / M. D. Larionova, S. V. Markova, N. V. Tikunova, E. S. Vysotski // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 14. - Ст. 4971. - P1-16, DOI 10.3390/ijms21144971 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Immunoassay -- Single-chain antibody -- Tick-borne encephalitis virus -- fusion protein -- glycoprotein -- histidine -- messenger RNA -- Metridia longa luciferase -- recombinant protein -- single chain fragment variable antibody -- unclassified drug -- amino terminal sequence -- antibody affinity -- antigen binding -- Article -- binding assay -- binding site -- bioluminescence -- bioluminescence resonance energy transfer -- cross reaction -- dissociation constant -- enzyme activity -- Escherichia coli -- gene -- genetic engineering -- genetic transfection -- immunoassay -- limit of detection -- mluc7 gene -- molecular cloning -- nonhuman -- nucleotide sequence -- protein expression -- protein purification -- protein unfolding -- spectral sensitivity -- tick borne encephalitis -- Tick borne encephalitis virus
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepod Metridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N-or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (KD = 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (KD = 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform of M. longa luciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Tikunova, N. V.; Vysotski, E. S.

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H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. -F. Chen, E. S. Vysotski, Y. -J. Liu // J Phys Chem B. - 2021, DOI 10.1021/acs.jpcb.1c03985 . - Article in press. - ISSN 1520-6106
Кл.слова (ненормированные):
Amino acids -- Excited states -- Hydrogen bonds -- Molecular dynamics -- Molecular modeling -- Molecules -- Phosphorescence -- Proton transfer -- Quantum theory -- Fast protons -- Marine organisms -- Photoproteins -- Primary products -- Proton transfer process -- Quantum mechanics/molecular mechanics -- Reaction substrates -- Singlet excited state -- Theoretical calculations -- Transfer channel -- Bioluminescence
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S1) is the emitter of CaRP. The S1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs. © 2021 American Chemical Society.

Scopus
Держатели документа:
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, Shanghai, 201418, China
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Center for Advanced Materials Research, Advanced Institute of Natural Sciences, Beijing Normal University at Zhuhai, Zhuhai, 519087, China
Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, 100875, China

Доп.точки доступа:
Chen, S. -F.; Vysotski, E. S.; Liu, Y. -J.

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H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. F. Chen, E. S. Vysotski, Y. J. Liu // J. Phys. Chem. B. - 2021. - Vol. 125, Is. 37. - P10452-10458, DOI 10.1021/acs.jpcb.1c03985. - Cited References:50. - This work was supported by the Program of Shanghai Institute of Technology (no. YJ2016-42), the National Natural Science Foundation of China (21973005 and 21911530094), and the Russian Foundation for Basic Research (20-04-00085 and 19-14-53004). . - ISSN 1520-6106. - ISSN 1520-5207

РУБ Chemistry, Physical
Рубрики:
CHEMILUMINESCENT DECOMPOSITION
   FLUORESCENCE-SPECTRA
   MECHANISM
   QM/MM
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S-1) is the emitter of CaRP. The S-1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S-1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S-1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S-1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S-1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs.

WOS
Держатели документа:
Shanghai Inst Technol, Sch Chem & Environm Engn, Shanghai 201418, Peoples R China.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Beijing Normal Univ Zhuhai, Ctr Adv Mat Res, Adv Inst Nat Sci, Zhuhai 519087, Peoples R China.
Beijing Normal Univ, Coll Chem, Key Lab Theoret & Computat Photochem, Minist Educ, Beijing 100875, Peoples R China.

Доп.точки доступа:
Chen, Shu-Feng; Vysotski, Eugene S.; Liu, Ya-Jun; Vysotski, Eugene; Program of Shanghai Institute of Technology [YJ2016-42]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21973005, 21911530094]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 19-14-53004]

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