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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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Illarionova V.A., Vysotski E.S.
Заглавие : Use of proZZ-obelin fusion protein in bioluminescent immunoassay
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1996. - Vol. 219, Is. 2. - С. 475-479. - 5. - ISSN 0006-291X, DOI 10.1006/bbrc.1996.0258
Примечания : Cited References: 21
Предметные рубрики: ESCHERICHIA-COLI
EXPRESSION
AEQUORIN
PURIFICATION
SYSTEM
Аннотация: Obelin is a photoprotein that emits light by Ca2+-binding. To develop a bioluminescent immunoassay based on the light emission property of obelin, we have expressed the apoobelin fusion protein with ZZ-domain of S. aureus protein A in E. coil by recombinant DNA techniques. The pro2Z-obelin expressed was purified by one-step affinity chromatography on IgG-Agarose. The purified proZZ-obelin has both the luminescent activity of obelin and the IgG-binding ability of ZZ-domain. The specific activity of fusion protein was 8.5 x 10(15) photons per mg of protein. (C) 1996 Academic Press, Inc.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana, V, Tikunova, Nina, V, Vysotski, Eugene S.
Заглавие : The Smallest Isoform ofMetridia longaLuciferase as a Fusion Partner for Hybrid Proteins
Колич.характеристики :16 с
Коллективы : Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; ICBFM SB RAS [AAAA-A17-117020210027-9]; Government of Krasnoyarsk Territory
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 14. - Ст.4971. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21144971
Примечания : Cited References:49. - The reported study was funded by the Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (S.V.M, M.D.L., and E.S.V.) and by the Russian State funded budget project of ICBFM SB RAS No. AAAA-A17-117020210027-9 (N.V.T.).
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
BIOLUMINESCENT REPORTER
GAUSSIA
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepodMetridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N- or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (K-D= 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (K-D= 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform ofM. longaluciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova M. D., Markova S. V., Tikunova N. V., Vysotski E. S.
Заглавие : The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 14. - Ст.4971. - С. 1-16. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21144971
Аннотация: Bioluminescent proteins are widely used as reporter molecules in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepod Metridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N-or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (KD = 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (KD = 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform of M. longa luciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya, Vasilisa V., Goncharova, Natalia S., Biriukov, Vladislav V., Bashmakova, Eugenia E., Kabilov, Marsel R., Baykov, Ivan K., Sokolov, Aleksey E., Frank, Ludmila A.
Заглавие : The Ca2+-Regulated Photoprotein Obelin as a Tool for SELEX Monitoring and DNA Aptamer Affinity Evaluation
Колич.характеристики :6 с
Коллективы : Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [18-38-00531]
Место публикации : Photochem. Photobiol.: WILEY, 2020. - Article in press. - ISSN 0031-8655, DOI 10.1111/php.13274. - ISSN 1751-1097(eISSN)
Примечания : Cited References:25. - This work has been supported by the Russian Foundation for Basic Research (RFBR) under the grant no 18-38-00531.
Предметные рубрики: CARDIAC TROPONIN-I
BIOLUMINESCENCE
IMMUNOASSAY
APTASENSOR
DIAGNOSIS
Аннотация: Bioluminescent solid-phase analysis was proposed to monitor the selection process and to determine binding characteristics of the aptamer-target complexes during design and development of the specific aptamers. The assay involves Ca2+-regulated photoprotein obelin as a simple, sensitive and fast reporter. Applicability and the prospects of the approach were exemplified by identification of DNA aptamers to cardiac troponin I, a highly specific early biomarker for acute myocardial infarction. Two structurally different aptamers specific to various epitopes of troponin I were obtained and then tested in a model bioluminescent assay.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bashmakova, Eugenia E., Krasitskaya, Vasilisa V., Frank, Ludmila A.
Заглавие : Simultaneous Genotyping of Four Single Nucleotide Polymorphisms Associated with Risk Factors of Hemostasis Disorders
Колич.характеристики :7 с
Коллективы : Russian Science Foundation [14-14-01119]
Место публикации : Comb. Chem. High Throughput Screen: BENTHAM SCIENCE PUBL LTD, 2015. - Vol. 18, Is. 10. - С. 930-936. - ISSN 1386-2073, DOI 10.2174/1386207318666150917095903. - ISSN 1875-5402(eISSN)
Примечания : Cited References:20. - The study was supported by the grant 14-14-01119 of the Russian Science Foundation.
Предметные рубрики: ALLELE-SPECIFIC PCR
FACTOR-V-LEIDEN
BIOLUMINESCENT IMMUNOASSAY
Ключевые слова (''Своб.индексиров.''): snp detection--pext reaction--photoprotein obelin--bioluminescent--microassay--multiplex pcr
Аннотация: Multiplex simultaneous genotyping technique was developed for four polymorphisms in genes coding for blood coagulation factors and homocysteine metabolism which are considered as thrombophilia related mutations: FV Leiden, FII G20210A, MTHFR C677T, and FVII G10976A. It is based on primer extension reaction with the following bioluminescent solid-phase microassay. At that, two different in bioluminescence obelin mutants were applied to simultaneous detection of two gene allelic variants. The assay is carried out in microtiter plate format and provides fast and reliable genotyping of four single nucleotide polymorphisms in four different genes within 2.5 hours. A large number of clinical samples were analyzed and the obtained results were found to be in complete correlation with those obtained by using conventional RT-PCR techniques.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryavtsev A.N., Krasitskaya V.V., Petunin A.I., Burakov A.Y., Frank L.A.
Заглавие : Simultaneous Bioluminescent Immunoassay of Serum Total and IgG-Bound Prolactins
Колич.характеристики :6 с
Место публикации : Anal. Chem.: AMER CHEMICAL SOC, 2012. - Vol. 84, Is. 7. - С. 3119-3124. - ISSN 0003-2700, DOI 10.1021/ac300444w
Примечания : Cited References: 10. - This work was supported in part by Grant No. 76 of the Russian Academy of Sciences, Siberian Branch and by the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (Grant No 11. G34.31.058).
Предметные рубрики: PHOTOPROTEIN OBELIN
POLYETHYLENE-GLYCOL
MACROPROLACTINEMIA
PRECIPITATION
VALIDATION
Аннотация: Novel dual-analyte single-well bioluminescence immunoassay (BLIA) for total and IgG-bound prolactins was developed on the base of Ca2+-regulated photoprotein obelin mutants with altered color and kinetics of bioluminescence signal as reporters. The mutants W92F-H22E and Y138F were chemically conjugated with monoclonal mouse anti-hPRL and anti-hIgG immunoglobulins and thus displayed signals from total prolactin and IgG-bounded prolactin (macroprolactin) correspondingly. Bioluminescence of the reporters was simultaneously triggered by a single injection of Ca2+ solution and discriminated via bioluminescent signal spectral and time resolution. The developed microplate-based immunoassay allows detection of two prolactin forms in crude serum without additional manipulations (e.g., gel chromatography or PEG-precipitation). Total prolactin bioluminescence immunoassay in standard, control, and clinical sera offers high sensitivity and reproducibility. The BLIA results show good correlation with those obtained by RIA and immunoassay after gel chromatography.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Borisova V.V., Frank L.A., Malikova N.P., Stepanyuk G.A., Markova S.V., Lee J..., Vysotski E.S.
Заглавие : Obelin mutants with altered colour of light emission as labels for dual-wavelength immunoassay
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2006. - Vol. 21, Is. 5. - С. 271-271. - ISSN 1522-7235
Примечания : Cited References: 0
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bashmakova, Eugenia E., Panamarev, Nikita S., Kudryavtsev, Alexander N., Frank, Ludmila A.
Заглавие : N-extended photoprotein obelin to competitively detect small protein tumor markers
Колич.характеристики :5 с
Коллективы : Russian Federation for young scientists [MK-772.2020.4]; Government of Krasnoyarsk Territory, Krasnoyarsk Regional Science Foundation [2021012006966]
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2022. - Vol. 598. - С. 69-73. - ISSN 0006-291X, DOI 10.1016/j.bbrc.2022.02.011. - ISSN 1090-2104(eISSN)
Примечания : Cited References:15. - The work was partially supported by a grant of the President of the Russian Federation for young scientists, the candidates of sciences (project MK-772.2020.4, study of a hybrid protein with melanoma-inhibiting activity) and Government of Krasnoyarsk Territory, Krasnoyarsk Regional Science Foundation (project No 2021012006966, study of a hybrid with protein survivin).
Предметные рубрики: MELANOMA INHIBITORY-ACTIVITY
SURVIVIN
Аннотация: Two variants of Ca2+-regulated photoprotein obelin, extended from the N-terminus with small tumor markers-melanoma inhibitory activity protein (MIA) and survivin, one of the protein inhibitors of apoptosis, were designed, obtained and studied. Both domains in the obtained hybrid proteins exhibit the properties of the initial molecules: the main features of Ca2+-triggered bioluminescence are close to those of obelin, and the tumor markers' domains are recognized and bound by the corresponding antibodies. The obtained hybrids compete with the corresponding tumor markers for binding with antibodies, immobilized on the surface and their use has been shown to be promising as bioluminescent labels in a one-stage solid-phase competitive immunoassay. (c) 2022 Published by Elsevier Inc.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Burakova L.P., Krasitskaya V.V., Kudryavtsev A.N., Shimomura O..., Frank L.A.
Заглавие : Hydrogen-bond networks between the C-terminus and Arg from the first alpha-helix stabilize photoprotein molecules
Колич.характеристики :7 с
Коллективы : RFBR [12-04-00753-a]; Government of Russian Federation [11.G34.31.0058]
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2014. - Vol. 13, Is. 3. - С. 541-547. - ISSN 1474-905X, DOI 10.1039/c3pp50369k. - ISSN 1474-9092
Примечания : Cited References: 22. - The work was supported by RFBR grant 12-04-00753-a, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058).
Предметные рубрики: GREEN FLUORESCENT PROTEIN
CA2+-REGULATED PHOTOPROTEIN
BIOLUMINESCENT IMMUNOASSAY
COELENTERAZINE BINDING
ANGSTROM RESOLUTION
ENERGY-TRANSFER
FUSION PROTEIN
APO-OBELIN
AEQUORIN
EXPRESSION
Аннотация: Previous studies have stated that aequorin loses most of its bioluminescence activity upon modification of the C-terminus, thus limiting the production of photoprotein fusion proteins at its N-terminus. In the present work, we investigate the importance of the C-terminal proline and the hydrogen bonds it forms for photoprotein active complex formation, stability and functional activity. According to the crystal structures of obelin and aequorin, two Ca2+-regulated photoproteins, the carboxyl group of the C-terminal Pro forms two hydrogen bonds with the side chain of Arg21 (Arg15 in aequorin case) situated in the first a-helix. Whereas, deletion or substitution of the C-terminal proline could noticeably change the bioluminescence activity, stability or the yield of an active photoprotein complex. Therefore, modifications of the first alpha-helix Arg has a clear destructive effect on the main photoprotein properties. A C-terminal hydrogen-bond network is proposed to be important for the stability of photoprotein molecules towards external disturbances, when taking part in the formation of locked protein conformations and isolation of coelenterazine-binding cavities.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryavtsev A.N., Krasitskaya V.V., Frank L.A.
Заглавие : Dual-analyte single-well bioluminescence immunoassay based on obelin color mutants
Колич.характеристики :2 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2012. - Vol. 27, Is. 2. - С. 131-132. - ISSN 1522-7235
Примечания : Cited References: 2
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12.

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).
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13.

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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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Markova S.V., Frank L.A.
Заглавие : Calcium-regulated photoproteins of marine coelenterates
Колич.характеристики :13 с
Место публикации : Mol. Biol.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2006. - Vol. 40, Is. 3. - С. 355-367. - ISSN 0026-8933, DOI 10.1134/S0026893306030022
Примечания : Cited References: 99
Предметные рубрики: BIOLUMINOMETRIC HYBRIDIZATION ASSAYS
HYDROID OBELIA-GENICULATA
GREEN-FLUORESCENT PROTEIN
POLYMERASE-CHAIN-REACTION
BIOLUMINESCENT IMMUNOASSAY
RECOMBINANT AEQUORIN
CRYSTAL-STRUCTURE
BIOTINYLATED AEQUORIN
ANGSTROM RESOLUTION
CA2+-REGULATED PHOTOPROTEINS
Ключевые слова (''Своб.индексиров.''): bioluminescence--obelin--aequorin--intracellular calcium--molecular diagnosis
Аннотация: Calcium-regulated photoproteins are bioluminescent proteins that are responsible for the luminescence of marine coelenterates. A photoprotein molecule is a stable enzyme-substrate complex consisting of a single polypeptide chain and an oxygen-preactivated substrate, 2-hydroperoxcoelenterazine, which is tightly but noncovalently bound with the protein. Bioluminescence is triggered by Ca2+ and results from decarboxylation of the substrate bound with the protein. This review considers the current information about the structure of photoproteins, the mechanism of the bioluminescent reaction, the function of particular amino acid residues of the active center in catalysis and the formation of the emitter, and the use of photoproteins in bioluminescent microanalysis.
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15.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Frank L.A., Borisova V.V., Vysotski E...
Заглавие : Calcium-regulated photoprotein obelin as a label in immunoassay: An outlook for applications
Колич.характеристики :4 с
Место публикации : Bioluminescence & Chemiluminescence: Progress and Perspectives: WORLD SCIENTIFIC PUBL CO PTE LTD, 2005. - 13th International Symposium on Bioluminescence and Chemiluminescence (AUG 02-06, 2004, Yokohama, JAPAN). - P463-466. - ISBN 981-256-118-8, DOI 10.1142/9789812702203_0110
Примечания : Cited References: 7
Предметные рубрики: BIOLUMINESCENT IMMUNOASSAY
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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) : Frank L.A.
Заглавие : Ca2+-Regulated Photoproteins: Effective Immunoassay Reporters
Колич.характеристики :14 с
Коллективы :
Место публикации : Sensors: MDPI AG, 2010. - Vol. 10, Is. 12. - С. 11287-11300. - ISSN 1424-8220, DOI 10.3390/s101211287
Примечания : Cited References: 70. - This work was supported by the grant No. 76 of the Russian Academy of Sciences, Siberian Branch.
Предметные рубрики: POLYMERASE-CHAIN-REACTION
CYTOKINE MESSENGER-RNA
BIOLUMINESCENT IMMUNOASSAY
MYCOBACTERIUM-TUBERCULOSIS
BIOTINYLATED AEQUORIN
RECOMBINANT AEQUORIN
ANGSTROM RESOLUTION
FUSION PROTEIN
PCR ASSAY
OBELIN
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-regulated photoprotein--immunoassay--pcr-elisa--multiplex assay--re-engineered photoproteins
Аннотация: Ca2+-regulated photoproteins of luminous marine coelenterates are of interest and a challenge for researchers as a unique bioluminescent system and as a promising analytical instrument for both in vivo and in vitro applications. The proteins are comprehensively studied as to biochemical properties, tertiary structures, bioluminescence mechanism, etc. This knowledge, along with available recombinant proteins serves the basis for development of unique bioluminescent detection systems that are "self-contained", triggerable, fast, highly sensitive, and non-hazardous. In the paper, we focus on the use of photoproteins as reporters in binding assays based on immunological recognition element-bioluminescent immunoassay and hybridization immunoassay, their advantages and prospects.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L..., Markova S..., Remmel N..., Vysotski E..., Gitelson I...
Заглавие : Bioluminescent signal system: bioluminescence immunoassay of pathogenic organisms
Колич.характеристики :6 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2007. - Vol. 22, Is. 3. - С. 215-220. - ISSN 1522-7235, DOI 10.1002/bio.952
Примечания : Cited References: 14
Предметные рубрики: AEQUORIN
AGENTS
OBELIN
ASSAYS
LABEL
Ключевые слова (''Своб.индексиров.''): obelin--bioluminescence immunoassay--infective agents
Аннотация: The Ca2+-regulated photoprotein obelin has been examined as a label for bioluminescence immunoassay of infective agents. The hepatitis B virus (HbsAg) and the bacteria Escherichia coli and Shigella sonnei lipopolysaccharide (LPS) were chosen as model antigens. Chemically synthesized obelin-corresponding antibody conjugates were used in a solid-phase microplate immunoassay. The sensitivities achieved by the assay were 0.25 ng/mL for S. sonnei LPS and 0.375 ng/mL for HbsAg. A novel, filter-based immunoassay to determine bacterial admixtures in the environment was proposed. The NanoCeram filters were effectively applied to 'trap' and pre-concentrate pathogens from samples under study for the purposes of further detection and measurement of the absorbed material by bioluminescence immunoassay. Copyright (C) 2007 John Wiley & Sons, Ltd.
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19.

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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20.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Frank L.A., Vysotski E.S.
Заглавие : Bioluminescent immunoassay of alphafetoprotein with Ca2+-activated photoprotein obelin
Место публикации : BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS: JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - С. 439-442. - 4. - ISBN 0-471-97502-8
Примечания : Cited References: 0
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