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^a343.17.09.05^2VINITI
Л 94

Люминесценция Ca{2}{+}-активируемого фотопротеина обелина под действием активных форм кислорода [Текст] : научное издание / Е. С. Высоцкий [и др.] // Докл. АН СССР. - 1991. - Т. 321, N 4. - С. 850-854 . - ISSN 0002-3264

ГРНТИ

34.17.09

РУБ 343.17.09.05
Рубрики:
БЕЛОК
   ОБЕЛИН
   КАЛЬЦИЙ-АКТИВИРУЕМЫЙ
   ЛЮМИНЕСЦЕНЦИЯ
   КИСЛОРОД АКТИВНЫЙ
   КИШЕЧНОПОЛОСТНЫЕ
   PROTEIN
   LUMINESCENCE
   ACTION OXYGEN
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Высоцкий, Евгений Степанович; Бондарь, Владимир Станиславович; Трофимов, К. П.; Гительзон, Иосиф Исаевич

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^a343.17.09.05^2VINITI
Б 81

Бондарь, В. С.
Люминесценция in vitro экстрактов из полихет Arotonoe vittata [Текст] : научное издание / В. С. Бондарь, С. В. Вологина, Е. С. Высоцкий ; Академия наук СССР. Сибирское отделение. Институт биофизики, АН СССР. СО. Ин-т биофиз. // Препр. - 1991. - N 164. - С. 1-17

ГРНТИ

34.17.09

РУБ 343.17.09.05
Рубрики:
ЛЮМИНЕСЦЕНЦИЯ
   ПОЛИХЕТЫ
   ЭКСТРАКТЫ
   LUMINESCENCE
Аннотация: Исследована люминесценция экстрактов из полихет Arotonoe vittata. Но гомогенатах, полученных из элитр животных, показано, что биолюминесцентная система полихет данного вида относится к фотопротеиновому типу и стимулируется in vitro как О[2]{-} при использовании реагентов Фентона, так и при {-}ОС1 анионом при использовании гипохлорита натрия. Определены величины K[m] для реагентов Фентона в люминесцентной реакции, которые составили 0,37 мМ для FeSO[4] и 8,20 мМ для Н[2]О[2]. Аскорбат (1 и 10 мМ) ингибировал люминесценцию, инициированную реагентами Фентона, тогда как диэтилдитиокарбамат (0,1; 1,0 и 10 мМ) - увеличивал. Показано, что люминесценция экстрактов протекает с существенно большим квантовым выходом при стимуляции ее {-}OCl анионом по сравнению с О[2]{-}. Константы псевдопервого порядка спада люминесцентной реакции составили 0,34 с{-1} для NaOCl и 5,63 с{-1} для реагентов Фентона. Ни аскорбат, ни диэтилдитиокарбамат практически не влияли на люминесценцию, инициированную гипохлоритом натрия
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Вологина, С.В.; Высоцкий, Е.С.; Академия наук СССР. Сибирское отделение. Институт биофизики

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Why does the bioluminescent fungus Armillaria mellea have luminous mycelium but nonluminous fruiting body? / K. V. Purtov [et al.] // Doklad. Biochem. Biophys. - 2017. - Vol. 474, Is. 1. - P217-219, DOI 10.1134/S1607672917030176 . - ISSN 1607-6729
Аннотация: By determining the components involved in the bioluminescence process in luminous and nonluminous organs of the honey fungus Armillaria mellea, we have established causes of partial luminescence of this fungus. The complete set of enzymes and substrates required for bioluminescence is formed only in the mycelium and only under the conditions of free oxygen access. Since the synthesis of luciferin precursor (hispidin) and 3-hydroxyhispidin hydroxylase in the fruiting bodies is blocked, the formation of luciferin—the key component of fungal bioluminescent system—was not observed. That is why the fruiting body of Armillaria mellea is nonluminous despite the presence of luciferase, the enzyme that catalyzes the oxidation of luciferin with a photon emission. © 2017, Pleiades Publishing, Ltd.

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Держатели документа:
Institute of Biophysics, Krasnoyarsk Research Center, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Purtov, K. V.; Petushkov, V. N.; Rodionova, N. S.; Gitelson, J. I.

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Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species [Text] / E. S. Vysotski [et al.] // Biochemistry. - 2003. - Vol. 42, Is. 20. - P6013-6024, DOI 10.1021/bi027258h. - Cited References: 45 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CALCIUM
   LUMINESCENCE
   LONGISSIMA
   EVOLUTION
   PROTEINS
   COELENTERAZINE
Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA USA
RAS, SB, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia
Univ Washington, Friday Harbor Labs, Seattle, WA 98195 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Liu, Z.J.; Markova, S.V.; Blinks, J.R.; Deng, L...; Frank, L.A.; Herko, M...; Malikova, N.P.; Rose, J.P.; Wang, B.C.; Lee, J...

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Use of bioluminescent enzyme system to detect antioxidant activity of fullerenol C60Oy(OH)(x) [Text] / A. . Tarasova [et al.] // Luminescence. - 2014. - Vol. 29. - P100-101. - Cited References: 6 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Tarasova, Anna
Kovel, Ekaterina] Siberian Fed Univ, Krasnoyarsk, Russia
[Tarasova, Anna
Kudryasheva, Nadezhda] Inst Biophys SB RAS, Krasnoyarsk, Russia
[Churilov, Grigoriy
Vnukova, Natalia
Isakova, Victoria
Osipova, Irina] Inst Phys SB RAS, Krasnoyarsk, Russia
ИБФ СО РАН
ИФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tarasova, A...; Kudryasheva, N...; Kovel, E...; Churilov, G...; Vnukova, N...; Isakova, V...; Osipova, I...

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Upper electron-excited states in bioluminescence: experimental indication [Text] / N. S. Kudryasheva [et al.] // Luminescence. - 2001. - Vol. 16, Is. 3. - P. 243-246, DOI 10.1002/bio.613. - Cited References: 22 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bioluminescence -- upper electron-excited states -- energy transfer
Аннотация: The involvement of upper electron-excited states in bacterial bioluminescence process was studied with excitation energy-accepting molecules. The fluorescent aromatic compounds, anthracene and 1.4-bis(5-phenyloxazol-2-yl)benzene, were chosen. Energies of their lowest excited singlet states are higher than the energy of the analogous state of the bioluminescence emitter; their absorption spectra and bioluminescence do not overlap. Hence, the excitation of these molecules by singlet-singlet energy transfer or by light absorption is excluded. Sensitized fluorescence of these compounds in the bioluminescence systems has been recorded, indicating the activity of upper electron-excited states in the bioluminescent process. Copyright (C) 2001 John Wiley & Sons, Ltd.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, SB, Krasnoyarsk 660036, Russia
Novosibirsk State Tech Univ, Novosibirsk 630092, Russia
Krasnoyarsk State Univ, Dept Phys, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Nemtseva, E.V.; Meshalkin, Y.P.; Sizykh, A.G.

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UNDERWAY MEASUREMENT OF BIOMINESCENT FIELD DURING BIOLOGICAL EXPEDITION [Текст] / I. I. GITELSON, R. N. UTYUSHEV, A. V. SHELEGOV // Okeanologiya. - 1991. - Vol. 31, Is. 4. - P. 631-637. - Cited References: 5 . - ISSN 0030-1574

РУБ Oceanography

Аннотация: Data on surface bioluminescence intensity measurements during the 15-th cruise of R/V Vityaz, January to March 1988, in the Indian Ocean, the Mediterranean and Black Seas are presented. High luminescence intensity is found in the Arabian and Black Seas and the Dardanelles. Recommendations on underway measurements of biological and hydrophysical parameters are given.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
GITELSON, I.I.; UTYUSHEV, R.N.; SHELEGOV, A.V.

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Ultrastructure and morphology of the bioluminescent system in "bioluminescent" and "non-bioluminescent" scale-worms (Polychaeta, Polynoidae) [Text] / N. B. Aneli [et al.] // Luminescence. - 2014. - Vol. 29. - P41-42. - Cited References: 5 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
ORGANS

WOS
Держатели документа:
[Aneli, N. B.] Russian Acad Sci EZAN, Expt Factory Sci Engn, Chernogolovka, Moscow Region, Russia
[Belousova, A. A.] Moscow MV Lomonosov State Univ, Fac Biol, Dept Invertebrate Zool, Moscow, Russia
[Saprunova, V. B.] Moscow MV Lomonosov State Univ, AN Belozersky Inst Physicochem Biol, Moscow, Russia
[Petushkov, V. N.] Russian Acad Sci, Siberian Branch, Lab Photobiol, Inst Biophys, Krasnoyarsk, Russia
[Kondrashov, F. A.
Plyuscheva, M. V.] CRG, Barcelona, Spain
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Aneli, N.B.; Belousova, A.A.; Saprunova, V.B.; Petushkov, V.N.; Kondrashov, F.A.; Plyuscheva, M.V.

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Two new types of bioluminescent systems of soil enchytraeids (Annelida:Clitellata:Oligochaeta:Enchytraeidae) / V. N. Petushkov, N. S. Rodionova // Doklady Akademii Nauk. - 2005. - Vol. 401, Is. 2. - С. 263-266 . - ISSN 0869-5652
Кл.слова (ненормированные):
Analysis -- Luminescence -- Models -- Soils -- Bioluminescent systems -- Oligochaeta earth-worm -- Biology
Аннотация: For the first time comparative data on localization, structural-functional organization, optimal functioning conditions for two bioluminescent systems of soil enchytraeids Fridericia heliota and Henlea sp. are given. Strong difference of these systems from each other and from all known among Oligochaeta class is shown. The analysis allows stating the discovery of two new systems of bioluminescent systems of enchytraeids, and accounting peroxide-dependent system of Diplocardia longa megascolecid, establishing multiplicity of luminescent mechanisms for Oligochaeta earth-worm.

Scopus
Держатели документа:
Inst. Biofiziki SO RAN, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Rodionova, N.S.

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10.

Two forms of substrate for the bioluminescent reaction in three species of basidiomycetes / A. P. Puzyr [et al.] // Mycol. - 2019. - Vol. 10, Is. 2. - P84-91, DOI 10.1080/21501203.2019.1583688 . - ISSN 2150-1203
Кл.слова (ненормированные):
Cold and hot extracts -- culture liquid -- enzymatic system -- hispidin -- luminous fungi -- substrate of luminescent reaction
Аннотация: The luminescent response of the enzymatic system of Armillaria borealis on the cold and hot extracts from cell-free culture liquids of Inonotus obliquus, Pholiota sp. and A. borealis was examined. The greatest influence on the light emission produced by the luminescent system of A. borealis was provided by the temperature at which the probes were prepared for assay. Boiling a culture liquid on water bath for a few minutes promoted a multifold increase in the luminescence. The results of luminescence assay suggest that the substance involved in the bioluminescent reaction in higher fungi is presented in culture liquids and mycelia in two forms. In one form, it is ready to interact with the enzymatic system and in the second form, it becomes accessible for the reaction after heat treatment. The pool of thermoactivated substance was found to be much large than the amount of the ready accessible one. We suggest that predecessors of hispidin, which is fungal luciferin precursor, are responsible for this phenomenon. They are not involved in bioluminescence at their original state and are converted into the substrate under the influence of high temperature. © 2019, © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

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Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Institute of Computational Technologies, Siberian Branch of Russian Academy of Science, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Burov, A. E.; Medvedeva, S. E.; Burova, O. G.; Bondar, V. S.

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11.

Transfer of xenobiotics through cell membranes of luminous bacteria / S. E. Medvedeva // Luminescence. - 1999. - Vol. 14, Is. 5. - P267-270 . - ISSN 1522-7235
Кл.слова (ненормированные):
Luminous bacteria -- Toxicant -- Ultrastructure -- bacterial DNA -- edetic acid -- toluene -- xenobiotic agent -- article -- cell membrane -- DNA damage -- drug effect -- luminescence -- metabolism -- Photobacterium -- sensitivity and specificity -- transport at the cellular level -- ultrastructure -- Vibrio -- Biological Transport -- Cell Membrane -- DNA Damage -- DNA, Bacterial -- Edetic Acid -- Luminescence -- Photobacterium -- Sensitivity and Specificity -- Toluene -- Vibrio -- Xenobiotics
Аннотация: The influence of some chemical substances on luminous bacteria was studied to elucidate the interrelation between the xenobiotics action on bacterial luminescence and cell ultrastructure. Such substances as quinones, phenols, chlorides of heavy metals (in concentrations of substances inhibiting luminescence by 50%) resulted in damaging effects upon bacteria: a lot of cells had damage of membranes due to changes in their permeability. It was found that the high concentration of EDTA and toluene decreased the luminescence and caused the condensation of DNA-fibrils and the cell damage after long-term and short-term action. The low concentration of EDTA and toluene did not decrease the bacterial luminescence; the noticeable damage of cell membranes did not take place during short-term treatment. However, the long action of these substances changed the membrane permeability resulting in increased sensitivity of bacterial luminescence to some toxic substances. Copyright В© 1999 John Wiley & Sons, Ltd.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Medvedeva, S.E.

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12.

Total peroxidase and catalase activity of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in comparison with the level of light emission [Text] / O. A. Mogil'naya [et al.] // Appl. Biochem. Microbiol. - 2015. - Vol. 51, Is. 4. - P419-424, DOI 10.1134/S0003683815040110. - Cited References:35. - The authors are grateful to N. V. Psurtseva (curator of the collection of basidiomycetes of the Botanical Institute, Russian Academy of Science) for help with the species affiliation of the IBSO 2328 culture. This work was supported by the Program of Interdisciplinary Projects of the Siberian Branch of the Russian Academy of Sciences, project no. 71. . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
OXIDATIVE STRESS
   SYSTEM
   FUNGI
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
basidiomycetes -- luminescence -- peroxidase -- catalase
Аннотация: The peroxidase and catalase activities in the mycelium of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in normal conditions and under stress were compared. An increase in the luminescence level was observed under stress, as well as an increase in peroxidase and catalase activities. Moreover, the peroxidase activity in extracts of A. borealis mycelium was found to be almost one and a half orders of magnitude lower, and the catalase activity more than two orders of magnitude higher in comparison with the N. nambi mycelium. It can be suggested that the difference between the brightly luminescent and dimly luminescent mycelium of N. nambi is due to the content of (HO2)-O-2 or other peroxide compounds.

WOS,
Scopus
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogil'naya, O. A.; Ronzhin, N. O.; Medvedeva, S. E.; Bondar', V. S.; Siberian Branch of the Russian Academy of Sciences [71]

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13.

Three-dimensional structures of mutants of Ca2+-regulated photoprotein obelin provide insight into molecular mechanisms underlying changes in bioluminescent properties [Text] / P. . Natashin, E. . Vysotski, Z. J. Liu // Luminescence. - 2014. - Vol. 29. - P36-36. - Cited References: 2 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Natashin, Pavel
Vysotski, Eugene] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
[Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China
[Natashin, Pavel
Vysotski, Eugene] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk, Russia
[Liu, Zhi-Jie] Shanghai Tech Univ, iHuman Inst, Shanghai, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P...; Vysotski, E...; Liu, Z.J.

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14.

The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - P774-779, DOI 10.1006/bbrc.1995.1880 . - ISSN 0006-291X
Кл.слова (ненормированные):
riboflavin -- article -- bioluminescence -- fluorescence -- nonhuman -- priority journal -- protein analysis -- protein synthesis -- vibrio -- vibrionaceae -- Bacterial Proteins -- Chromatography, Gel -- Chromatography, Thin Layer -- Flavin Mononucleotide -- Flavoproteins -- Luminescence -- Riboflavin -- Spectrometry, Fluorescence -- Support, U.S. Gov't, P.H.S. -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Vibrio -- Vibrio fischeri
Аннотация: The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore. Both forms are active for shifting the bioluminescence spectral maximum. The fluorescence spectral distribution of the two proteins differs slightly and the in vivo emission appears to be an equal mixture of the two. The bioluminescence activity of the riboflavin Y1 protein contrasts with the inactivity of the related Photobacterium type.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J.

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15.

THE WAY OF SYNTHESIS OF LUCIFERASE ALDEHYDE FACTOR IN PHOTOBACTERIUM MANDAPAMENSIS AND THE INFLUENCE OF ALDEHYDE PRECURSORS ON THE LUMINESCENCE DEVELOPMENT [Текст] / A. N. SHENDEROV, L. Y. POPOVA // Genetika. - 1980. - Vol. 16, Is. 6. - P. 1109-1112. - Cited References: 7 . - ISSN 0016-6758

РУБ Genetics & Heredity

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
SHENDEROV, A.N.; POPOVA, L.Y.

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16.

The use of glowing wood as a source of luminescent culture of fungus mycelium [Text] / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2016. - Vol. 7, Is. 1. - P1-17, DOI 10.5943/mycosphere/7/1/1. - Cited References:22. - The authors are grateful to Prof. A. Frank, Director of North Borneo Biostation, for the opportunity to carry out studies of glowing wood; to Nadezhda N. Kudashova, a senior researcher at the Institute of Biology and Biophysics at the Tomsk University, for identifying the species of nonluminous fungi. This study was supported by grant no. 11.G34.31.0058 (RF Government) and Projects no. 71 (SB RAS). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
BIOLUMINESCENCE CHARACTERISTICS
NEONOTHOPANUS-NAMBI
LIGHT-EMISSION
Кл.слова (ненормированные):
Bioluminescence -- culture of luminous mycelia -- kinetics of luminescent -- reaction -- light emitting wood -- luminous fungus
Аннотация: In studies of fungal bioluminescence, not only fruiting bodies and spores of the fungus, but also samples of luminescent wood, leaf litter or soil may need to be used to derive pure mycelial culture. This study describes an approach to isolating the culture of luminescent fungal mycelium from samples of light-emitting wood found on Borneo Island in November-December 2013. A GelDoc XR Imaging System (Bio-Rad Laboratories, Inc., U.S.) was used for the first time to monitor luminescence and select luminous samples. This study shows that for successful isolation of the culture of luminescent mycelium out of the luminescent wood found in the forest, it is imperative to keep the samples moist (mycelium alive until there is water), while immediate and aseptic delivery of the samples to the laboratory is not a crucial condition (inner layers of wood is "sterile"). Investigation of the growth features of the isolated mycelium in various growing conditions revealed some peculiar properties of its luminescence in comparison with the known luminescent cultures of basidiomycetes. When grown on solid nutrient media, mycelium exhibits low growth rates, long-lasting luminescence (140 days or longer), and emergence and disappearance of local zones with high levels of light emission. Mycelium produced in submerged culture does not emit light, and this effect must be caused by the absence or a very low level of the luminescent reaction substrate in the biomass. The luminescence system isolated from mycelial biomass did not induce luminescent reaction in vitro upon the addition of NADPH (recording intensity is 60 100 URL/sec). We found that enzymes of the luminescence systems isolated from mycelium pellets retained their activity and catalyzed luminescent reaction when a hot extract of the luminous fungus Armillaria sp. (IBSO 2360) was added (near 1900 URL/sec). The same effect was obtained after addition of hot extracts from the fruiting bodies of nonluminous higher fungi Pholiota squarrosa, Cortinarius sp., Hypholoma capnoides and Chroogomphus rutilus (near 3500 URL/sec). The pure culture of luminescent mycelium has been registered in the Culture Collection of IBP SB RAS as IBSO 2371; now it can be used for various in vivo and in vitro studies, including identification of the fungus.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Bondar, V. S.; RF Government [11.G34.31.0058]; SB RAS [71]

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РУБ Biochemistry & Molecular Biology

Держатели документа:
[Tomilin, F. N.
Antipina, L. U.
Ovchinnikov, S. G.] SB RAS, LV Kirensky Phys Inst, Krasnoyarsk 660036, Russia
[Vysotski, E. S.] SB RAS, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
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Держатели документа:
[Lee, J.
Vysotski, E. S.] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Vysotski, E. S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
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Bayer HealthCare, Global Drug Discovery Target Res, D-42096 Wuppertal, Germany
Univ Georgia, Dept Mol Biol & Biochem, Athens, GA 30602 USA
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