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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН
Иностранные журналы библиотеки Института биофизики СО РАН
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1.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., BONDAR V.S., ILLARIONOVA V.A., VYSOTSKI E.S.
Заглавие : SEQUENCE OF THE CDNA-ENCODING THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Gene: ELSEVIER SCIENCE BV, 1995. - Vol. 153, Is. 2. - С. 273-274. - 2. - ISSN 0378-1119, DOI 10.1016/0378-1119(94)00797-V
Примечания : Cited References: 6
Предметные рубрики: CA-2+-ACTIVATED PHOTOPROTEIN
AEQUORIN
CLONING
Ключевые слова (''Своб.индексиров.''): bioluminescence--calcium--gene--plasmid--marine coelenterates
Аннотация: A cDNA clone encoding the Ca2+-activated photoprotein, obelin (Obl), from Obelia longissima was sequenced. The nucleotide (nt) sequence contained two long overlapping open reading frames (ORFs), one of which encoded apoobelin (apoObl). The deduced amino acid (aa) sequence of apoObl revealed that this 195-aa protein has three EF-hand structures that are characteristic for Ca2+-binding domains. Strong aa homology was shown among apoObl, apoaequorin and apoclytin. The second ORF present in the obl cDNA consists of 139 codons and encodes a very basic protein with a calculated pI of 10.56 and a molecular mass of 16153 Da.
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2.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., MARKOVA S.V., BONDAR V.S., VYSOTSKY E.S., GITELSON J.I.
Заглавие : ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA
Место публикации : Dokl. Akad. Nauk: MEZHDUNARODNAYA KNIGA, 1992. - Vol. 326, Is. 5. - С. 911-913. - 3. - ISSN 0869-5652
Примечания : Cited References: 12
Предметные рубрики: AEQUORIN
PROTEIN
PHIALIDIN
CLONING
CA-2+
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3.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Vysotski E.S.
Заглавие : Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase
Колич.характеристики :4 с
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2013. - Vol. 450, Is. 1. - С. 147-150. - ISSN 1607-6729, DOI 10.1134/S1607672913030095
Примечания : Cited References: 14. - This work was supported by the Ministry of Education and Science of the Russian Federation (Government Contract no. 16.512.11.2141) and Council of the President of the Russian Federation on Grants and State Support of Leading Scientific Schools (project no. NSh-64987.2010.4).
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
GENE-EXPRESSION
CDNA
CLONING
BIOLUMINESCENCE
RENIFORMIS
Scopus
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4.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Frank L.A., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin
Колич.характеристики :9 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2013. - Vol. 12, Is. 6. - С. 1016-1024. - ISSN 1474-905X, DOI 10.1039/c3pp00002h
Примечания : Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
CA2+-BINDING PHOTOPROTEIN
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
MNEMIOPSIS-LEIDYI
LIGHT-EMISSION
W92F OBELIN
CLONING
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.
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5.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stepanyuk G.A., Unch J..., Malikova N.P., Markova S.V., Lee J..., Vysotski E.S.
Заглавие : Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase
Колич.характеристики :9 с
Коллективы :
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2010. - Vol. 398, Is. 4. - С. 1809-1817. - ISSN 1618-2642, DOI 10.1007/s00216-010-4106-9
Примечания : Cited References: 39. - This work was supported by grant 09-04-12022 of the Russian Foundation for Basic Research, "Molecular and Cell Biology" program of Russian Academy of Sciences, by the SB RAS grant No. 2, and by the SB RAS Lavrentiev grant for Young Scientists.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
BIOLUMINESCENT REPORTER
CA2+-REGULATED PHOTOPROTEINS
RENIFORMIS LUCIFERASE
RECOMBINANT OBELIN
GENE-EXPRESSION
IN-VIVO
CDNA
CLONING
PURIFICATION
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--calcium--imaging
Аннотация: It has been shown that the coelenterazine analog, coelenterazine-v, is an efficient substrate for a reaction catalyzed by Renilla luciferase. The resulting bioluminescence emission maximum is shifted to a longer wavelength up to 40 nm, which allows the use of some "yellow" Renilla luciferase mutants for in vivo imaging. However, the utility of coelenterazine-v in small-animal imaging has been hampered by its instability in solution and in biological tissues. To overcome this drawback, we ligated coelenterazine-v to Ca2+-triggered coelenterazine-binding protein from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The coelenterazine-v bound within coelenterazine-binding protein has revealed a greater long-term stability at both 4 and 37 degrees C. In addition, the coelenterazine-binding protein ligated by coelenterazine-v yields twice the total light over free coelenterazine-v as a substrate for the red-shifted R. muelleri luciferase. These findings suggest the possibility for effective application of coelenterazine-v in various in vitro assays.
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6.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Borisova V.V., Frank L.A., Markova S.V., Burakova L.P., Vysotski E.S.
Заглавие : Recombinant Metridia luciferase isoforms: expression, refolding and applicability for in vitro assay
Колич.характеристики :7 с
Коллективы :
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2008. - Vol. 7, Is. 9. - С. 1025-1031. - ISSN 1474-905X, DOI 10.1039/b807271j
Примечания : Cited References: 19. - The work was supported by Bayer AG, by the Russian Foundation for Basic Research grants 05-04-48271 and 06-04-08076, by the joint grant 06-04-89502 of the Russian Foundation for Basic Research and Taiwan National Science Council, and by the "Molecular and Cellular Biology" program of the Russian Academy of Sciences.
Предметные рубрики: BIOLUMINESCENT REPORTER
GAUSSIA LUCIFERASE
CDNA
PROTEINS
CLONING
OVEREXPRESSION
PURIFICATION
MUTAGENESIS
ENZYME
OBELIN
Аннотация: The recombinant coelenterazine-dependent luciferases (isoforms MLuc 164 and MLuc39) from the marine copepod Metridia longa were expressed as inclusion bodies in E. coli cells, dissolved in 6 M guanidinium chloride and folded in conditions developed for proteins containing intramolecular disulfide bonds. One of them (MLuc09) was obtained in an active monomeric form with a high yield. The luciferase bioluminescence is found to be initiated not only by free coelenterazine, but also by Ca2+-dependent coelenterazine-binding protein (CBP) of Renilla muelleri on Ca2+ addition. The use of CBP as a "substrate" provides higher light emission and simultaneously the lower level of background. The high purity MLuc39 can be detected down to attomol with a linear range extending over 5 orders of magnitude. The MLuc39 reveals also a high stability towards heating and chemical modification; the chemically synthesized biotinylated derivatives of the luciferase preserve 35-40% of the initial activity The luciferase applicability as an in vitro bioluminescent reporter is demonstrated in model tandem bioluminescent solid-phase microassay combining the Ca2+-regulated photoprotein obelin and the Metridia luciferase.
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7.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Borisova V.V., Markova S.V., Malikova N.P., Stepanyuk G.A., Vysotski E.S.
Заглавие : Violet and greenish photoprotein obelin mutants for reporter applications in dual-color assay
Колич.характеристики :6 с
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2008. - Vol. 391, Is. 8. - С. 2891-2896. - ISSN 1618-2642, DOI 10.1007/s00216-008-2223-5
Примечания : Cited References: 22
Предметные рубрики: ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CRYSTAL-STRUCTURE
BIOLUMINESCENCE
AEQUORIN
IMMUNOASSAY
EXPRESSION
CDNA
PURIFICATION
CLONING
Ключевые слова (''Своб.индексиров.''): ca(2+)-regulated photoprotein--bioluminescence--dual-color assay
Аннотация: Two kinds of Ca(2+)-regulated photoprotein obelin with altered color of bioluminescence were obtained by active-center amino acid substitution. The mutant W92F-H22E emits violet light (lambda(max)=390 nm) and the mutant Y139F emits greenish light (lambda (max)=498 nm), with small spectral overlap, both display high activity and stability and thus may be used as reporters. For demonstration, the mutants were applied in dual-color simultaneous immunoassay of two gonadotropic hormones-follicle-stimulating hormone and luteinizing hormone. Bioluminescence of the reporters was simultaneously triggered by single injection of Ca(2+) solution, divided using band-pass optical filters and measured with a two-channel photometer. The sensitivity of simultaneous bioluminescence assay was close to that of a separate radioimmunoassay.
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8.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Vysotski E.S., Markova S.V., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin
Колич.характеристики :13 с
Место публикации : Protein Sci.: COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, 2005. - Vol. 14, Is. 3. - С. 663-675. - ISSN 0961-8368, DOI 10.1110/ps.041142905
Примечания : Cited References: 46
Предметные рубрики: RAY CRYSTALLOGRAPHIC ANALYSIS
ANGSTROM RESOLUTION
SEQUENCE-ANALYSIS
CA2+-REGULATED PHOTOPROTEINS
CA2+-DISCHARGED PHOTOPROTEIN
LUMINESCENT PROTEIN
MODULATED PROTEINS
ELECTRON-DENSITY
CLONING
CDNA
Ключевые слова (''Своб.индексиров.''): bioluminescence--ef-hand--fluorescent protein--proton relay--calcium-binding loops--aequorin--obelin--diffraction
Аннотация: The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7 Angstrom and 2.2 Angstrom. respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-proteins retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hydroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these subtle shifts are the basis of the ability of these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.
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9.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Markova S.V., Vysotski E.S., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : Preparation and X-ray crystallographic analysis of the Ca2+-discharged photoprotein obelin
Колич.характеристики :3 с
Место публикации : Acta Crystallogr. Sect. D-Biol. Crystallogr.: BLACKWELL MUNKSGAARD, 2004. - Vol. 60. - С. 512-514. - ISSN 0907-4449, DOI 10.1107/S090744490302852X
Примечания : Cited References: 18
Предметные рубрики: VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
W92F OBELIN
AEQUORIN
SEQUENCE
PROTEIN
CLONING
CDNA
Аннотация: Ca2+-regulated photoproteins belong to the EF-hand Ca2+-binding protein family. The addition of calcium ions initiates bright blue bioluminescence of the photoproteins, a result of the oxidative breakdown of coelenterazine peroxide to coelenteramide. Crystals of the Ca2+-discharged W92F mutant of obelin from Obelia longissima have been grown, representing the first crystallization of a photoprotein after the Ca2+-triggered bioluminescence. A green fluorescence observed from the crystals clearly demonstrates that coelenteramide, the bioluminescence product of coelenterazine peroxide, is bound within the protein. The diffraction pattern exhibits tetragonal Laue symmetry. Systematic absences indicate that the space group is either P4(3)2(1)2 or P4(1)2(1)2. The unit-cell parameters are a=b=53.4, c=144.0 Angstrom. The crystals diffract to 1.9 Angstrom resolution.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Stepanyuk G.A., Frank L.A., Markova S.V., Vysotski E.S., Lee J...
Заглавие : Spectral tuning of obelin bioluminescence by mutations of Trp92
Колич.характеристики :5 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2003. - Vol. 554, Is. 01.02.2013. - С. 184-188. - ISSN 0014-5793, DOI 10.1016/S0014-5793(03)01166-9
Примечания : Cited References: 13
Предметные рубрики: VIOLET BIOLUMINESCENCE
W92F OBELIN
AEQUORIN
PURIFICATION
EXPRESSION
EMISSION
CLONING
Ключевые слова (''Своб.индексиров.''): photoprotein--aequorin--calcium--fluorescence
Аннотация: The Ca2+-regulated photoprotein obelin was substituted at Trp92 by His, Lys, Glu, and Arg. All mutants fold into stable conformations and produce bimodal bioluminescence spectra with enhanced contribution from a violet emission. The W92R mutant has an almost monomodal bioluminescence (lambda(max)=390 nm) and monomodal fluorescence (lambda(max)=425 nm) of the product. Results are interpreted by an excited state proton transfer mechanism involving the substituent side group and His22 in the binding cavity. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Berestovskaya N.G., Shaloiko L.A., Gorokhovatsky A.Y., Bondar V.S., Vysotski E.S., Maximov J.E., von Doehren H..., Alakhov Y.B.
Заглавие : Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC, 1999. - Vol. 268, Is. 1. - С. 72-78. - ISSN 0003-2697, DOI 10.1006/abio.1998.3051
Примечания : Cited References: 22
Предметные рубрики: SEQUENCE-ANALYSIS
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
LIGHT-EMISSION
AEQUORIN
CDNA
CLONING
EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : MATVEEV S.V., ILLARIONOV B.A., VYSOTSKI E.S., BONDAR V.S., MARKOVA S.V., ALAKHOV Y.B.
Заглавие : OBELIN MESSENGER-RNA - A NEW TOOL FOR STUDIES OF TRANSLATION IN CELL-FREE SYSTEMS
Колич.характеристики :6 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1995. - Vol. 231, Is. 1. - С. 34-39. - ISSN 0003-2697, DOI 10.1006/abio.1995.1499
Примечания : Cited References: 17
Предметные рубрики: MESSENGER-RNA
AEQUORIN
PROTEIN
CLONING
CDNA
Аннотация: Obelin mRNA obtained in vitro with the aid of SP6 RNA polymerase was translated in a wheat germ cell-free system, Only the polypeptide with a molecular mass of about 20 kDa was synthesized. The activation of apoobelin with a synthetic coelenterazine revealed a luminescence activity initiated by calcium. The specific activity was 3.6 +/- 0.4 x 10(15) photons per mg of the in vitro synthesized obelin (k = 6.9 s(-1)). The luminescence of the obelin was in a good correlation with the protein concentration calculated by the incorporation of [C-14]Leu. The determination of the amount of de novo synthesized obelin based on measurement of its luminescence is one-thousand times more sensitive than the approach based on the incorporation of labeled amino acid. Thus, obelin mRNA has some advantages for evaluating the efficiency of cell-free translation when compared with standard methods. (C) 1995 Academic Press, Inc.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bondar V.S., Purtov K.V., Malikova N.P., Frank L.A., Illarionov B.A.
Заглавие : Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: MAIK NAUKA/INTERPERIODICA, 2001. - Vol. 66, Is. 9. - С. 1014-1018. - ISSN 0006-2979, DOI 10.1023/A:1012377827626
Примечания : Cited References: 21
Предметные рубрики: CDNA
EXPRESSION
AEQUORIN
SEQUENCE
CLONING
Ключевые слова (''Своб.индексиров.''): photoproteins--obelin--apoobelin mutants--bioluminescence
Аннотация: Using site directed mutagenesis, the conservative residue Cys158 of recombinant apoobelin was substituted for sera ine (C158S, S-mutant) or alanine (C158A, A-mutant). These point mutations resulted in significant changes in the apoobelin structure accompanied by slowing of photoprotein complex formation, decrease of its stability, and changing of its bioluminescence characteristics. The enzymatic properties of the photoprotein decreased in the series: wild-type protein S-mutant A-mutant. This is consistent with rank of nucleophilicity SH OH CH3 of cysteine, serine, and alanine side chain functional groups, respectively. Possible mechanisms of the involvement of the apoobelin Cys158 SH-group in the formation of the enzyme-substrate complex are considered.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., MARKOVA S.V., BONDAR V.S., VYSOTSKY E.S., GITELSON J.I.
Заглавие : ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA
Колич.характеристики :3 с
Место публикации : Dokl. Akad. Nauk: MEZHDUNARODNAYA KNIGA, 1992. - Vol. 326, Is. 5. - С. 911-913. - ISSN 0869-5652
Примечания : Cited References: 12
Предметные рубрики: AEQUORIN
PROTEIN
PHIALIDIN
CLONING
CA-2+
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V.V., Burakova L.P., Pyshnaya I.A., Frank L.A.
Заглавие : Bioluminescent reporters for identification of gene allelic variants
Колич.характеристики :8 с
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2012. - Vol. 38, Is. 3. - С. 298-305. - ISSN 1068-1620, DOI 10.1134/S1068162012030090
Примечания : Cited References: 13. - The authors thank the staff of Hematology Research Center (Krasnoyarsk Branch of Russian Academy of Medical Sciences) for providing DNA samples. The work was supported by the Integration Interdisciplinary Project of Siberian Branch of the Russian Academy of Sciences No. 76 and the Krasno yarsk Regional Fund for the support of scientific and technological activities.
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
RENILLA-MUELLERI
LUCIFERASE
PURIFICATION
SUBSTRATE
CLONING
CDNA
Ключевые слова (''Своб.индексиров.''): snp--pext reaction--obelin--luciferase--bioluminescent microassay
Аннотация: A method for single nucleotide polymorphism identification was developed, which was based on the primer extension reaction (PEXT) followed by bioluminescent solid-phase microassay. Recombinant Ca2+-regulated photoprotein obelin and coelenterazine-dependent Renilla muelleri luciferase were used as reporters. The study was performed as an example of SNP genotyping of the human F5 gene encoding human Factor V Leiden polymorphism 1691 G - A (R506Q). Genomic DNA was amplified by PCR using primers flanking polymorphic site of 140 base pairs. PCR products were used as templates for two PEXT reactions using two primers containing 3'-terminal nucleotides, which were complementary to either normal or mutant alleles. If the template and allele-specific primer were completely complementary, the latter was elongated with DNA polymerase. The resulting extension product contained biotin residue due to the presence of biotinylated deoxyuridine triphosphate (B-dUTP) in the reaction mixture. The products were analyzed using obelin-streptavidin conjugates. The optimal PEXT-reaction conditions were found, which ensured a high reliability of SNP genotyping. A new approach to simultaneously revealing both alleles in one well was developed using two bioluminescent reporters. The efficiency of the proposed approach was shown in the study of clinical DNA samples.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya V.V., Korneeva S.I., Kudryavtsev A.N., Markova S.V., Stepanyuk G.A., Frank L.A.
Заглавие : Ca2+-triggered coelenterazine-binding protein from Renilla as an enzyme-dependent label for binding assay
Колич.характеристики :7 с
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2011. - Vol. 401, Is. 8. - С. 2573-2579. - ISSN 1618-2642, DOI 10.1007/s00216-011-5343-2
Примечания : Cited References: 17. - The work was supported by a "Leading Scientific School" (N 64987.2010.4) grant from the President of the Russian Federation and the "Molecular and Cell Biology" Program from the RAS.
Предметные рубрики: BIOLUMINESCENT IMMUNOASSAY
LUCIFERASE
PURIFICATION
RENIFORMIS
MUELLERI
OBELIN
PHOTOPROTEIN
EXPRESSION
SUBSTRATE
CLONING
Ключевые слова (''Своб.индексиров.''): ca2+-triggered coelenterazine-binding protein (cbp)--renilla muelleri luciferase--bioluminescent solid-phase microassay
Аннотация: The recombinant Ca2+-triggered coelenterazine-binding protein (CBP) from Renilla muelleri was investigated as a biospecifically labeled molecule for in vitro assay applications. The protein was shown to be stable in solutions in the frozen state, as well as stable under heating and to chemical modifications. Conjugates with biotin, oligonucleotide, and proteins were obtained and applied as biospecific molecules in a solid-phase microassay. CBP detection was performed with intact (no modifications were made) Renilla luciferase in the presence of calcium, and the detection limit was found to be 75 amol. Model experiments indicate that this approach shows much promise, especially with regard to the development of multianalytical systems.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L..., Natashin P..., Markova S..., Eremeeva E..., Vysotsky E...
Заглавие : The C-terminal tyrosine deletion in mitrocomin increases its bioluminescent activity
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2014. - Vol. 29. - С. 84-84. - ISSN 1522-7235. - ISSN 1522-7243
Примечания : Cited References: 6
Предметные рубрики: PHOTOPROTEIN
EXPRESSION
AEQUORIN
CLONING
CDNA
WOS
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sandalova T.P., Ugarova N.N.
Заглавие : Model of the active site of firefly luciferase
Колич.характеристики :6 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1999. - Vol. 64, Is. 8. - P962-967. - ISSN 0006-2979
Примечания : Cited References: 20
Предметные рубрики: ESCHERICHIA-COLI
SEQUENCE
CLONING
ENZYME
CDNA
SUPERFAMILY
Ключевые слова (''Своб.индексиров.''): bioluminescence--firefly luciferase--atp--luciferin--spatial structure--active site--enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.
WOS
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Berestovskaya N.G., Shaloiko L.A., Gorokhovatsky A.Y., Bondar V.S., Vysotski E.S., Maximov J.E., von Doehren H..., Alakhov Y.B.
Заглавие : Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC, 1999. - Vol. 268, Is. 1. - P72-78. - ISSN 0003-2697, DOI 10.1006/abio.1998.3051
Примечания : Cited References: 22
Предметные рубрики: SEQUENCE-ANALYSIS
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
LIGHT-EMISSION
AEQUORIN
CDNA
CLONING
EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.
WOS
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T.G., Kalacheva G.S., Gorbunova O.V., Zhila N.O.
Заглавие : Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786
Колич.характеристики :8 с
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA, 2004. - Vol. 40, Is. 2. - P170-177. - ISSN 0003-6838, DOI 10.1023/B:ABIM.0000018921.04863.d5
Примечания : Cited References: 27
Предметные рубрики: POLY-BETA-HYDROXYBUTYRATE
ORGANISM ALCALIGENES-EUTROPHUS
ESCHERICHIA-COLI
PHB
POLY(3-HYDROXYBUTYRATE)
BIOSYNTHESIS
CLONING
GENES
CHAIN
H16
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.
WOS
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