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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Puzyr' A. P., Pozdnyakova I. O., Bondar' V. S.
Заглавие : Design of a luminescent biochip with nanodiamonds and bacterial luciferase
Место публикации : Phys. Solid State: AMER INST PHYSICS, 2004. - Vol. 46, Is. 4. - P761-763. - ISSN 1063-7834, DOI 10.1134/1.1711469
Примечания : Cited References: 10
Аннотация: An "aluminum oxide film-adhesive layer-nanodiamond-luciferase" supramolecular structure is prepared on a flat plate. It is demonstrated that, in this structure, the enzyme retains the catalytic activity. The structure prepared can be treated as a luminescent biochip prototype for use in bioluminescent analysis. (C) 2004 MAIK "Nauka / Interperiodica".
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bondarenko L. S., Kovel E. S., Kydralieva K. A., Dzhardimalieva G. I., Illes E., Tombacz E., Kicheeva A. G., Kudryasheva N. S.
Заглавие : Effects of modified magnetite nanoparticles on bacterial cells and enzyme reactions
Место публикации : Nanomaterials. - 2020. - Vol. 10, Is. 8. - Ст.1499. - P.1-20. - ISSN 20794991 (ISSN), DOI 10.3390/nano10081499
Примечания : Cited References: 83. - This research was funded by the Russian Foundation for Basic Research (#19-315-50048, #19-33-90149, and #18-29-19003)
Аннотация: Current paper presents biological effects of magnetite nanoparticles (MNPs). Analyzing effects of MNP’ characteristics (zeta-potential and hydrodynamic diameters) on bacteria and their enzyme reactions was the main focus. Photobacterium phosphoreum and bacterial enzymatic reactions were chosen as bioassays. Three types of MNPs were under study: bare Fe3O4, Fe3O4 modified with 3-aminopropyltriethoxysilane (Fe3O4/APTES), and humic acids (Fe3O4/HA). Effects of the MNPs were studied at a low concentration range (< 2 mg/L) and attributed to availability and oxidative activity of Fe3+, high negative surface charge, and low hydrodynamic diameter of Fe3O4/HA, as well as higher Fe3+ content in suspensions of Fe3O4/HA. Low-concentration suspensions of bare Fe3O4 provided inhibitory effects in both bacterial and enzymatic bioassays, whereas the MNPs with modified surface (Fe3O4/APTES and Fe3O4/HA) did not affect the enzymatic activity. Under oxidative stress (i.e., in the solutions of model oxidizer, 1,4-benzoquinone), MNPs did not reveal antioxidant activity, moreover, Fe3O4/HA demonstrated additional inhibitory activity. The study contributes to the deeper understanding of a role of humic substances and silica in biogeochemical cycling of iron. Bioluminescence assays, cellular and enzymatic, can serve as convenient tools to evaluate bioavailability of Fe3+ in natural dispersions of iron-containing nanoparticles, e.g., magnetite, ferrihydrite, etc.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Salnikov M. V., Medvedeva S. E., Petushkov V. N., Gitelzon I. I.
Заглавие : Electron-microscope study of the structure of luciferase from luminescent bacteria
Место публикации : Doklady Akademii Nauk. - 1981. - Vol. 261, Is. 5. - P.1254-1256. - ISSN 0002-3264
Примечания : Cited References: 4
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryavtsev, Alexander N., Krasitskaya, Vasilisa V., Efremov, Maxim K., Zangeeva, Sayana V., Rogova A. V., Tomilin F. N., Frank, Ludmila A.
Заглавие : Ca2+-triggered coelenterazine-binding protein Renilla: Expected and unexpected features
Место публикации : Int. J. Mol. Sci. - 2023. - Vol. 24, Is. 3. - Ст.2144. - ISSN 16616596 (ISSN), DOI 10.3390/ijms24032144. - ISSN 14220067 (eISSN)
Примечания : Cited References: 24. - This research was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, project No. 0287-2022-0002 and the Interagency Supercomputer Center of the Russian Academy of Sciences, MVS-100K and MVS-10P
Аннотация: Ca2+-triggered coelenterazine-binding protein (CBP) is a natural form of the luciferase substrate involved in the Renilla bioluminescence reaction. It is a stable complex of coelenterazine and apoprotein that, unlike coelenterazine, is soluble and stable in an aquatic environment and yields a significantly higher bioluminescent signal. This makes CBP a convenient substrate for luciferase-based in vitro assay. In search of a similar substrate form for the luciferase NanoLuc, a furimazine-apoCBP complex was prepared and verified against furimazine, coelenterazine, and CBP. Furimazine-apoCBP is relatively stable in solution and in a frozen or lyophilized state, but as distinct from CBP, its bioluminescence reaction with NanoLuc is independent of Ca2+. NanoLuc turned out to utilize all the four substrates under consideration. The pairs of CBP-NanoLuc and coelenterazine-NanoLuc generate bioluminescence with close efficiency. As for furimazine-apoCBP-NanoLuc pair, the efficiency with which it generates bioluminescence is almost twice lower than that of the furimazine-NanoLuc. The integral signal of the CBP-NanoLuc pair is only 22% lower than that of furimazine-NanoLuc. Thus, along with furimazine as the most effective NanoLuc substrate, CBP can also be recommended as a substrate for in vitro analytical application in view of its water solubility, stability, and Ca2+-triggering “character”.
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