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Труды сотрудников ИБФ СО РАН

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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Burakova L.P., Vysotski E.S.
Заглавие : High-active truncated luciferase of copepod Metridia longa
Колич.характеристики :6 с
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2012. - Vol. 417, Is. 1. - С. 98-103. - ISSN 0006-291X, DOI 10.1016/j.bbrc.2011.11.063
Примечания : Cited References: 31. - This study was supported by the Grants 16.512.11.2141 and 64987.2010.4 of the Ministry of Education and Science of Russian Federation.
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
REPORTER-GENE-EXPRESSION
RENILLA LUCIFERASE
GAUSSIA LUCIFERASE
LIGHT-EMITTER
IN-VIVO
BIOLUMINESCENCE
PHOTOPROTEINS
CDNA
SUBSTRATE
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--mammalian expression--secretion
Аннотация: The technology of real-time imaging in living cells is crucial for understanding of intracellular events. For this purpose, bioluminescent reporters have been introduced as sensitive and convenient tools. Metridia luciferase (MLuc) from the copepod Metridia longa is a coelenterazine-dependent luciferase containing a natural signal peptide for secretion. We report the high-active MLuc mutants with deletion of the N-terminal variable part of amino acid sequence. The MLuc variants were produced in Escherichia coil cells, converted to an active protein, and characterized. We demonstrate that the truncated MLucs have significantly increased bioluminescent activity as against the wild type enzyme but substantially retain other properties. One of the truncated variants of MLuc was transiently expressed in HEK 293 cells. The results clearly suggest that the truncated Metridia luciferase is well suited as a secreted reporter ensuring higher detection sensitivity in comparison with a wild type enzyme. (C) 2011 Elsevier Inc. All rights reserved.
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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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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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T.G., Kalacheva G.S., Altukhova O.V.
Заглавие : Autotrophic synthesis of polyhydroxyalkanoates by the bacteria Ralstonia eutropha in the presence of carbon monoxide
Колич.характеристики :4 с
Место публикации : Appl. Microbiol. Biotechnol.: SPRINGER-VERLAG, 2002. - Vol. 58, Is. 5. - P675-678. - ISSN 0175-7598, DOI 10.1007/s00253-002-0941-8
Примечания : Cited References: 35
Предметные рубрики: PSEUDOMONAS-OLEOVORANS
ALCALIGENES-EUTROPHUS
COAL
CULTIVATION
METABOLISM
SUBSTRATE
CULTURE
CO2
H-2
O-2
Аннотация: It has been found that the carbon monoxide (CO)-resistant strain of the hydrogen bacteria Ralstonia eutropha B5786 is able to synthesise polyhydroxyalkanoates (PHAs) in the presence of CO under autotrophic conditions. This strain, grown on model gas mixtures containing 5-25% CO v/v), accumulates up to 70-75% (of absolutely dry matter) PHA, without significant variation in the yield coefficient on hydrogen. No suppression of the activities of the key enzymes of PHA synthesis (beta-ketothiolase, acetoacetyl-CoA-reductase, butyrate dehydrogenase and poly-3-hydroxybutyrate synthase) was recorded. The PHA synthesised is a copolymer containing mostly beta-hydroxybutyrate (more than 99 mol%) with trace amounts of beta-hydroxyvalerate. The investigated properties of the polymer (molecular weight, crystallinity, temperature characteristics) do not differ from those of the polymer synthesised on electrolytic hydrogen.
WOS
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