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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Высоцкий, Евгений Степанович, Бондарь, Владимир Станиславович, Трофимов К. П., Гительзон, Иосиф Исаевич
Заглавие : Люминесценция Ca{2}{+}-активируемого фотопротеина обелина под действием активных форм кислорода : научное издание
Место публикации : Докл. АН СССР. - 1991. - Т. 321, N 4. - С. 850-854. - ISSN 0002-3264
ГРНТИ : 34.17.09
Предметные рубрики: БЕЛОК
ОБЕЛИН
КАЛЬЦИЙ-АКТИВИРУЕМЫЙ
ЛЮМИНЕСЦЕНЦИЯ
КИСЛОРОД АКТИВНЫЙ
КИШЕЧНОПОЛОСТНЫЕ
PROTEIN
LUMINESCENCE
ACTION OXYGEN
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., TROFIMOV K.P., VYSOTSKII E.S.
Заглавие : PHYSICOCHEMICAL PROPERTIES OF A PHOTOPROTEIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 10. - С. 1020-1027. - 8. - ISSN 0006-2979
Примечания : Cited References: 36
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
CA-2+
INDICATORS
PROTEIN
BINDING
PURIFICATION
EXTRACTION
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-activated photoprotein--obelin--chromatography--calcium
Аннотация: The photoprotein obelin was isolated and purified to homogeneity (as indicated by sodium dodecyl sulfate polyacrylamide gel electrophoresis) from hydroids of Obelia longissima by gel filtration on Sephadex G-75 fine, ion exchange chromatography on Polysil CA-300 (10 mum), hydrophobic chromatography on Phenyl-Sepharose CL-4B, gel filtration on Sephacryl S-200 superfine, ion exchange chromatography on a Mono Q column at pH 7.0, chromatofocusing on a Mono P column (pH gradient 6.0-4.0), and ion exchange chromatography on a Mono Q column at pH 5.5, 8.8, and 7.0. The molecular weight of the native protein was 30 kD, and that measured in the presence of SDS was 19.8 kD. The specific activity of obelin is 4.9.10(15) quanta/mg protein, pseudo-first-order constant of bioluminescence decay 4 sec-1, and quantum yield 0.16 The range of measurable Ca2+ concentrations is 10(-7) to 10(-5) M. The luminescence spectrum of obelin peaks at 469 nm, and the fluorescence emission maximum of the discharged protein is at 455 nm. The optimum pH for luminescence is between 9.0 and 10.5. The molecular ionization constants are pK1 6.8 and pK2 12.2, and the ionization constants for the active site are pK1 9.1 and pK2 10.2
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKI E.S., TROFIMOV C.P., BONDAR V.S., FRANK L.A., MARKOVA S.V., ILLARIONOV B.A.
Заглавие : MN2+-ACTIVATED LUMINESCENCE OF THE PHOTOPROTEIN OBELIN
Место публикации : Arch. Biochem. Biophys.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1995. - Vol. 316, Is. 1. - С. 92-99. - 8. - ISSN 0003-9861, DOI 10.1006/abbi.1995.1014
Примечания : Cited References: 38
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
CA-2+-ACTIVATED PHOTOPROTEIN
MESSENGER-RNA
BEROE-OVATA
AEQUORIN
PURIFICATION
PROTEIN
CDNA
EXTRACTION
Аннотация: The light emission of obelin may be initiated by Mn2+ under alkaline conditions. The luminescence takes place in a pH range from 7 to 12 with a sharp optimum at 11.75. The first-order rate constant for Mn2+-activated luminescence decay is more than 9 s(-1), while that for Ca2+-activated luminescence decay is only 6.9 s(-1). The Mn2+ concentration-effect curve for obelin determined with simple dilutions of manganese salt is a sigmoid curve, The slope of the curve is moderately dependent on the pH and was not more than 1 within the pH range tested. The maximal light emission, which is initiated by 3.6 X 10(-5) M Mn2+ at pH 11.75 was about 10% of the maximal Ca2+-activated luminescence. Mg2+ ions inhibit the Mn2+-activated luminescence of obelin. The addition of OH. and O-2(-) scavengers did not influence the Mn2+-activated luminescence, but when singlet oxygen quenchers were added, the Mn2+-dependent light emission was inhibited. This suggests that the O-1(2) might be formed and itself be responsible for chromophore oxidation attended with light emission. NEM and Na2S2O4 inhibit the Mn2+-initiated light emission of obelin completely, showing that endogenous hydroperoxide and SH-group(s) of the photoprotein are essential for both Ca2+-activated and Mn2+-activated light emission of obelin. (C) 1995 Academic Press, Inc.
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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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Antipina L.Y., Tomilin F.N., Vysotskii E.S., Ovchinnikov S.G.
Заглавие : A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN
Колич.характеристики :6 с
Место публикации : J. Struct. Chem.: SPRINGER, 2011. - Vol. 52, Is. 5. - С. 870-875. - ISSN 0022-4766
Примечания : Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213).
Предметные рубрики: CALCIUM-DISCHARGED OBELIN
SEMIEMPIRICAL METHODS
1.7 ANGSTROM
OPTIMIZATION
PARAMETERS
MECHANISM
FLUORESCENCE
ELEMENTS
PROTEIN
EMITTER
Ключевые слова (''Своб.индексиров.''): coelenterazine--2-hydroperoxy-coelenterazine--obelia longissima--renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Petunin A.I., Vysotski E.S.
Заглавие : Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay
Колич.характеристики :5 с
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA, 2004. - Vol. 30, Is. 4. - С. 327-331. - ISSN 1068-1620, DOI 10.1023/B:RUBI.0000037257.80835.7a
Примечания : Cited References: 16
Предметные рубрики: ESCHERICHIA-COLI
PURIFICATION
AEQUORIN
PROTEIN
CDNA
Ключевые слова (''Своб.индексиров.''): bioluminescent immunoassay--obelin--thyroid stimulating hormone
Аннотация: An efficient procedure for obelin conjugation with immunoglobulins was developed. The possibility was shown of using the resulting conjugates instead of a radioisotope label for the immunoassay of thyroid stimulating hormone in sera; the conjugates provide a sensitivity of 0.01 muIU/ml. The results of bioluminescent immunoassay (sera of 34 patients) satisfactorily correlate with the results of radioisotope assay (R 0.99).
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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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Petunin A.I., Vysotski E.S.
Заглавие : Bioluminescent immunoassay of thyrotropin and thyroxine using obelin as a label
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2004. - Vol. 325, Is. 2. - С. 240-246. - ISSN 0003-2697, DOI 10.1016/j.ab.2003.11.003
Примечания : Cited References: 16
Предметные рубрики: AEQUORIN
PURIFICATION
PROTEIN
CDNA
Ключевые слова (''Своб.индексиров.''): obelin--human thyrotropin--thyroxine--immunoassay--bioluminescence
Аннотация: Solid-phase bioluminescent immunoassay of thyroid hormones, human thyrotropin (hTSH) and two forms of thyroxine (T4), whose determinations are vitally important for diagnostics of thyroid diseases and the efficiency of treatment, is described. The recombinant obelin, a Ca2+-regulated photoprotein originally derived from the luminous marine hydroid Obelia longissima, is employed as a bioluminescent label. To produce obelin conjugates with anti-hTSH, anti-T4 immunoglobulins (IgG), and T4, additional SH groups are introduced into the obelin molecule using Traut's reagent (2-iminothiolane) and then obelin possessing extra SH groups is conjugated with succinimidyl 4-(N-maleimidomethyl)-cyclohexane-1-carboxylate-activated IgGs or T4. The total yield of obelin conjugates determined by luminescent activity is 60-65% after all chemical and purification procedures. The obtained conjugates are stable to lyophilization and in solution for at least 9 months at 4 degreesC, with loss of activity not exceeding 10%. The application of obelin conjugates for determination of the hTSH, total T4, and free T4 in standard, control, and patient sera displays high sensitivity and reproducibility of results. The results of bioluminescent immunoassays are closely comparable to those obtained by the radioimmunoassay method (R = 0.95-0.99). (C) 2003 Elsevier Inc. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarionov B.A., Frank L.A., Illarionova V.A., Bondar V.S., Vysotski E.S., Blinks J.R.
Заглавие : Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator
Колич.характеристики :27 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - С. 223-249. - ISSN 0076-6879
Примечания : Cited References: 58
Предметные рубрики: PHOTOPROTEIN OBELIN
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
DIRECTED MUTAGENESIS
SEQUENCE-ANALYSIS
HYDROID OBELIA
AEQUORIN
PROTEIN
BIOLUMINESCENCE
LUMINESCENCE
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Stepanyuk G.A., Vysotski E.S., Lee J..., Markova S.V., Malikova N.P., Wang B.C.
Заглавие : Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state
Колич.характеристики :6 с
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: NATL ACAD SCIENCES, 2006. - Vol. 103, Is. 8. - С. 2570-2575. - ISSN 0027-8424, DOI 10.1073/pnas.0511142103
Примечания : Cited References: 51
Предметные рубрики: X-RAY-DIFFRACTION
ANGSTROM RESOLUTION
CA2+-REGULATED PHOTOPROTEINS
AEQUORIN BIOLUMINESCENCE
VIOLET BIOLUMINESCENCE
W92F OBELIN
PROTEIN
LUCIFERASE
LIGHT
PROGRAM
Ключевые слова (''Своб.индексиров.''): coelenterazine--photoprotein--ef hand--luciferase--aequorin
Аннотация: The crystal structure at 1.93-angstrom resolution is determined for the Ca2+-discharged obelin containing three bound calcium ions as well as the product of the bioluminescence reaction, coelenteramide. This finding extends the series of available spatial structures of the ligand-dependent conformations of the protein to four, the obelin itself, and those after the bioluminescence reaction with or without bound Ca2+ and/or coelenteramide. Among these structures, global conformational changes are small, typical of the class of "calcium signal modulators" within the EF-hand protein superfamily. Nevertheless, in the active site there are significant repositions of two residues. The His-175 imidazole ring flips becoming almost perpendicular to the original orientation corroborating the crucial importance of this residue for triggering bioluminescence. Tyr-138 hydrogen bonded to the coelenterazine N1-atom in unreacted obelin is moved away from the binding cavity after reaction. However, this Tyr is displaced by a water molecule from within the cavity, which now forms a hydrogen bond to the same atom, the amide N of coelenteramide. From this observation, a reaction scheme is proposed that would result in the neutral coelenteramide as the primary excited state product in photoprotein bioluminescence. From such a higher energy state it is now energetically feasible to account for the shorter wavelength bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy state of the phenolate anion to yield the blue bioluminescence ordinarily observed from native photoproteins.
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11.

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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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKII Y.S., BONDAR V.S., GITELZON I.I.
Заглавие : ISOLATION AND PROPERTIES OF VARIOUS MOLECULAR-FORMS OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN
Колич.характеристики :4 с
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1991. - Vol. 321, Is. 1. - С. 214-217. - ISSN 0002-3264
Примечания : Cited References: 14
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
PROTEIN
PURIFICATION
EXTRACTION
PHIALIDIN
SEQUENCE
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13.

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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14.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Kargatova T.V., Boyandin A.N., Popova L.Y., Pechurkin N.S.
Заглавие : Experimental evaluation of the processes resulting from the introduction of the transgenic microorganism Escherichia coli Z905/pPHL7 (luk(+)) into aquatic microcosms
Колич.характеристики :6 с
Место публикации : SPACE LIFE SCIENCES: CLOSED ARTIFICIAL ECOSYSTEMS AND LIFE SUPPORT SYSTEMS. Ser. ADVANCES IN SPACE RESEARCH: PERGAMON-ELSEVIER SCIENCE LTD, 2003. - Vol. 31: Meeting of F4 1 Session of the 34th Scientific Assembly of COSPAR (OCT, 2002, HOUSTON, TEXAS), Is. 7. - P1769-1774. - ISBN 0273-1177, DOI 10.1016/S0273-1177(03)00119-4
Примечания : Cited References: 16
Предметные рубрики: SURVIVAL
PROTEIN
Аннотация: The processes resulting from the introduction of the transgenic microorganism (TM) E. coli Z905/pPHL7 into aquatic microcosms have been modeled experimentally. It has been shown that the TM E. coli is able to adapt to a long co-existence with indigenous heterotrophic microflora in variously structured microcosms. In more complex microcosms the numerical dynamics of the introduced E. coli Z905/pPHL7 population is more stable. In the TM populations staying in the microcosms for a prolonged time, changes are recorded in the phenotypic expression of plasmid genes (ampicillin resistance and the luminescence level) and chromosome genes (morphological and physiological traits). However, in our study microcosms, the recombinant plasmid persisted in the TM cells for 6 years after die introduction, and as the population adapts to the conditions of the microcosms, the efficiency of the cloned gene expression in the cells is restored. In the microcosms with high microalgal counts (10(7) cells/ml), cells with a high threshold of sensitivity to ampicillin dominate in the population of the TM E. coli Z905/pPHL7. (C) 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.
WOS
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Petunin A.I., Vysotski E.S.
Заглавие : Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay
Колич.характеристики :5 с
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA, 2004. - Vol. 30, Is. 4. - P327-331. - ISSN 1068-1620, DOI 10.1023/B:RUBI.0000037257.80835.7a
Примечания : Cited References: 16
Предметные рубрики: ESCHERICHIA-COLI
PURIFICATION
AEQUORIN
PROTEIN
CDNA
Ключевые слова (''Своб.индексиров.''): bioluminescent immunoassay--obelin--thyroid stimulating hormone
Аннотация: An efficient procedure for obelin conjugation with immunoglobulins was developed. The possibility was shown of using the resulting conjugates instead of a radioisotope label for the immunoassay of thyroid stimulating hormone in sera; the conjugates provide a sensitivity of 0.01 muIU/ml. The results of bioluminescent immunoassay (sera of 34 patients) satisfactorily correlate with the results of radioisotope assay (R 0.99).
WOS
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya O.A., Lobova T.I., Kargatova T.V., Popova L.Y.
Заглавие : Biofilm formation by bacterial associations under various salinities and copper ion stress
Колич.характеристики :9 с
Место публикации : Biofouling: TAYLOR & FRANCIS LTD, 2005. - Vol. 21, Is. 05.06.2013. - P247-255. - ISSN 0892-7014, DOI 10.1080/08924010500445848
Примечания : Cited References: 24
Предметные рубрики: HEAVY-METAL RESISTANCE
BACILLUS-SUBTILIS
PROTEIN
RISK
Ключевые слова (''Своб.индексиров.''): binary community--surface films--adhesion--copper--stress
Аннотация: The study addresses the effect of abiotic (medium salinity and copper ions) and biotic (interactions between populations) factors on the formation of structured communities by binary associations consisting of halotolerant bacteria (Alcaligenes sp. 1-1 or Acinetobacter sp. 1-19) and a wild-type B. subtilis 2335 strain or a transgenic strain. The results showed that 250 mg l(-1) of copper ions inhibit formation of biofilms by monocultures of the tested strains. Binary associations of the strains were more resistant to high concentrations (250 mg l(-1)) of copper ions. At the lowest NaCl concentration (0.05% and 2.5%) and in the presence of copper ions, bacilli seemed to help halotolerant bacteria survive. Under increased salinity and in the presence of copper ions, structured communities developed due to halotolerant bacteria. Coexistence under stressful conditions was beneficial for the both groups of bacteria.
WOS
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova, Svetlana V., Larionova, Marina D., Gorbunova, Darya A., Vysotski, Eugene S.
Заглавие : The disulfide-rich Metridia luciferase refolded from E. coli inclusion bodies reveals the properties of a native folded enzyme produced in insect cells
Колич.характеристики :7 с
Коллективы : RFBR; Government of Krasnoyarsk Territory [16-44-242099]; Russian Academy of Sciences [0356-2016-0712]
Место публикации : J. Photochem. Photobiol. B-Biol.: ELSEVIER SCIENCE SA, 2017. - Vol. 175. - С. 51-57. - ISSN 1011-1344, DOI 10.1016/j.jphotobiol.2017.08.024
Примечания : Cited References:30. - These studies were funded by RFBR and the Government of Krasnoyarsk Territory according to the research project No. 16-44-242099 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 0356-2016-0712).
Предметные рубрики: GAUSSIA-PRINCEPS LUCIFERASE
ESCHERICHIA-COLI
EXPRESSION
PROTEIN
Ключевые слова (''Своб.индексиров.''): copepod luciferase--disulfide bonds--cysteine-rich protein--oxidative--refolding
Аннотация: The bioluminescence of a marine copepod Metridia Tonga is determined by a small secreted coelenterazine-dependent luciferase that uses coelenterazine as a substrate of enzymatic reaction to generate light (lambda(max) = 480 nm). To date, four different isoforms of the luciferase differing in size, sequences, and properties have been cloned by functional screening. All of them contain ten conserved Cys residues that suggests up to five S-S intramolecular bonds per luciferase molecule. Whereas the use of copepod luciferases as bioluminescent reporters in biomedical research in vivo is growing from year to year, their application for in vitro assays is still limited by the difficulty in obtaining significant amounts of luciferase. The most cost-effective host for producing recombinant proteins is Escherichia coli. However, prokaryotic and eukaryotic cells maintain the reductive environment in cytoplasm that hinders the disulfide bond formation and consequently the proper folding of luciferase. Here we report the expression of the MLuc7 isoform of M. longa luciferase in E. colt cells and the efficient procedure for refolding from inclusion bodies yielding a high-active monomeric protein. Furthermore, in a set of identical experiments we demonstrate that bioluminescent and structural features of MLuc7 produced in bacterial cells are identical to those of MLuc7 isoform produced from culture medium of insect cells. Although the yield of high-purity protein is only 6 mg/L, the application of E. coil cells to produce the luciferase is simpler and more cost-effective than the use of insect cells. We expect that the suggested technology of Metridia luciferase production allows obtaining of sufficient amounts of protein both for the development of novel in vitro analytical assays with the use of MLuc7 as a label and for structural studies.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Davydova, Anna, Vorobyeva, Mariya, Bashmakova, Eugenia, Vorobjev, Pavel, Krasheninina, Olga, Tupikin, Alexey, Kabilov, Marsel, Krasitskaya, Vasilisa, Frank, Ludmila, Venyaminova, Alya
Заглавие : Development and characterization of novel 2 '-F-RNA aptamers specific to human total and glycated hemoglobins
Колич.характеристики :8 с
Коллективы : Russian Science Foundation [16-14-10296]
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2019. - Vol. 570. - С. 43-50. - ISSN 0003-2697, DOI 10.1016/j.ab.2019.02.004. - ISSN 1096-0309(eISSN)
Примечания : Cited References:32. - We want to thank Dr. Alexander Lomzov (ICBFM SB RAS) for his valuable assistance with circular dichroism studies. The work was supported by the Russian Science Foundation (grant number 16-14-10296).
Предметные рубрики: RNA APTAMER
SEQUENCES
PROTEIN
DNA
Аннотация: Aptamers are short DNA and RNA fragments which bind their molecular targets with affinity and specificity comparable to those of antibodies. Here, we describe the selection of novel 2'-F-RNA aptamers against total human hemoglobin or its glycated form HbA1c. After SELEX and high-throughput sequencing of the enriched libraries, affinities and specificities of candidate aptamers and their truncated variants were examined by the solid-phase bioluminescent assay. As a result, we identified aptamers specific to both hemoglobins or only glycated HbA1c. The developed 2'-F-RNA aptamers have shown their applicability for detection of total and glycated hemoglobin in one sample.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Dubinnyi, Maxim A., Ivanov, Igor A., Rodionova, Natalia S., Kovalchuk, Sergey I., Kaskova, Zinaida M., Petushkov, Valentin N.
Заглавие : alpha-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp.
Колич.характеристики :5 с
Коллективы : State Assignment for Basic Research of the Russian Academy of Sciences [0356-2019-0019]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-04-00348-a]
Место публикации : ChemistrySelect: WILEY-V C H VERLAG GMBH, 2020. - Vol. 5, Is. 42. - С. 13155-13159. - ISSN 2365-6549, DOI 10.1002/slct.202003075
Примечания : Cited References:49. - This work was supported by the State Assignment for Basic Research of the Russian Academy of Sciences (project no. 0356-2019-0019) and the Russian Foundation for Basic Research (project no. 19-04-00348-a).
Предметные рубрики: STRUCTURE ELUCIDATION
MANNOSYLATION
TRYPTOPHAN
PROTEIN
COMPLEMENT
Аннотация: Cold extract from bioluminescent earthworm Henlea sp. was studied by HPLC, 1D and 2D NMR and LC-HRMS analysis. An abundant structural analog of the luciferin was isolated and identified as alpha-C-mannosyltryptophan (ManTrp), the product of unusual C2-glycosylation found earlier in humans, ascidians and other animals. Two compounds in cold extract (P300b, P300c) were characterized as C2-substituted derivatives of tryptophan. We hypothesize that a series of tryptophan-containing compounds are possible participants of bioluminescence-related metabolism in Henlea sp.
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