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Violet and greenish photoprotein obelin mutants for reporter applications in dual-color assay [Text] / L. A. Frank [et al.] // Anal. Bioanal. Chem. - 2008. - Vol. 391, Is. 8. - P2891-2896, DOI 10.1007/s00216-008-2223-5. - Cited References: 22 . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE
   BIOLUMINESCENCE
   AEQUORIN
   IMMUNOASSAY
   EXPRESSION
   CDNA
   PURIFICATION
   CLONING
Кл.слова (ненормированные):
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.

Держатели документа:
[Frank, Ludmila A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Frank, Ludmila A.
Borisova, Vasilisa V.
Markova, Svetlana V.
Malikova, Natalia P.
Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Borisova, V.V.; Markova, S.V.; Malikova, N.P.; Stepanyuk, G.A.; Vysotski, E.S.

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Use of proZZ-obelin fusion protein in bioluminescent immunoassay [Text] / L. A. Frank, V. A. Illarionova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 1996. - Vol. 219, Is. 2. - P475-479, DOI 10.1006/bbrc.1996.0258. - Cited References: 21 . - 5. - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
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.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Illarionova, V.A.; Vysotski, E.S.

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The Smallest Isoform ofMetridia longaLuciferase as a Fusion Partner for Hybrid Proteins / M. D. Larionova, S. V. Markova, N. V. Tikunova, E. S. Vysotski // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 14. - Ст. 4971, DOI 10.3390/ijms21144971. - 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.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
COELENTERAZINE-BINDING PROTEIN
BIOLUMINESCENT REPORTER
GAUSSIA
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- copepod luciferase -- single-chain -- antibody -- immunoassay -- tick-borne encephalitis virus
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.

WOS
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.
Inst Chem Biol & Fundamental Med, Russian Acad Sci, Siberian Branch, Novosibirsk 630090, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana, V; Tikunova, Nina, V; Vysotski, Eugene S.; Vysotski, Eugene; 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

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The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins / M. D. Larionova, S. V. Markova, N. V. Tikunova, E. S. Vysotski // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 14. - Ст. 4971. - P1-16, DOI 10.3390/ijms21144971 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Immunoassay -- Single-chain antibody -- Tick-borne encephalitis virus -- fusion protein -- glycoprotein -- histidine -- messenger RNA -- Metridia longa luciferase -- recombinant protein -- single chain fragment variable antibody -- unclassified drug -- amino terminal sequence -- antibody affinity -- antigen binding -- Article -- binding assay -- binding site -- bioluminescence -- bioluminescence resonance energy transfer -- cross reaction -- dissociation constant -- enzyme activity -- Escherichia coli -- gene -- genetic engineering -- genetic transfection -- immunoassay -- limit of detection -- mluc7 gene -- molecular cloning -- nonhuman -- nucleotide sequence -- protein expression -- protein purification -- protein unfolding -- spectral sensitivity -- tick borne encephalitis -- Tick borne encephalitis virus
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
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Tikunova, N. V.; Vysotski, E. S.

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The Ca2+-Regulated Photoprotein Obelin as a Tool for SELEX Monitoring and DNA Aptamer Affinity Evaluation / V. V. Krasitskaya, N. S. Goncharova, V. V. Biriukov [et al.] // Photochem. Photobiol. - 2020, DOI 10.1111/php.13274. - Cited References:25. - This work has been supported by the Russian Foundation for Basic Research (RFBR) under the grant no 18-38-00531. . - Article in press. - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
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.

WOS
Держатели документа:
Fed Res Ctr KSC SB RAS, Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Inst Chem Biol & Fundamental Med SB RAS, Novosibirsk, Russia.
Fed Res Ctr KSC SB RAS, Kirensky Inst Phys, Krasnoyarsk, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Goncharova, Natalia S.; Biriukov, Vladislav V.; Bashmakova, Eugenia E.; Kabilov, Marsel R.; Baykov, Ivan K.; Sokolov, Aleksey E.; Frank, Ludmila A.; Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [18-38-00531]

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Simultaneous Genotyping of Four Single Nucleotide Polymorphisms Associated with Risk Factors of Hemostasis Disorders [Text] / E. E. Bashmakova, V. V. Krasitskaya, L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P930-936, DOI 10.2174/1386207318666150917095903. - Cited References:20. - The study was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
ALLELE-SPECIFIC PCR
FACTOR-V-LEIDEN
BIOLUMINESCENT IMMUNOASSAY
Кл.слова (ненормированные):
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.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Bashmakova, Eugenia E.; Krasitskaya, Vasilisa V.; Frank, Ludmila A.; Russian Science Foundation [14-14-01119]

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Simultaneous Bioluminescent Immunoassay of Serum Total and IgG-Bound Prolactins / A. N. Kudryavtsev [et al.] // Anal. Chem. - 2012. - Vol. 84, Is. 7. - P3119-3124, DOI 10.1021/ac300444w. - 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). . - ISSN 0003-2700

РУБ Chemistry, Analytical
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.

Держатели документа:
[Kudryavtsev, Alexander N.
Krasitskaya, Vasilisa V.
Frank, Ludmila A.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Kudryavtsev, Alexander N.
Krasitskaya, Vasilisa V.
Frank, Ludmila A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Petunin, Alexei I.] DIAS Ltd, Krasnoyarsk 660036, Russia
[Burakov, Andrey Y.] Krasnoyarsk Reg Hosp 1, Krasnoyarsk 660022, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryavtsev, A.N.; Krasitskaya, V.V.; Petunin, A.I.; Burakov, A.Y.; Frank, L.A.

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Obelin mutants with altered colour of light emission as labels for dual-wavelength immunoassay [Text] / V. V. Borisova [et al.] // Luminescence. - 2006. - Vol. 21, Is. 5. - P271-271. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
RAS, SB, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Mol Biol & Biochem, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Borisova, V.V.; Frank, L.A.; Malikova, N.P.; Stepanyuk, G.A.; Markova, S.V.; Lee, J...; Vysotski, E.S.

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N-extended photoprotein obelin to competitively detect small protein tumor markers / E. E. Bashmakova, N. S. Panamarev, A. N. Kudryavtsev, L. A. Frank // Biochem. Biophys. Res. Commun. - 2022. - Vol. 598. - P69-73, DOI 10.1016/j.bbrc.2022.02.011. - 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). . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MELANOMA INHIBITORY-ACTIVITY
SURVIVIN
Кл.слова (ненормированные):
Photoprotein obelin -- Genetic fusion -- Tumor marker -- Competitive assay
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.

WOS
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Bashmakova, Eugenia E.; Panamarev, Nikita S.; Kudryavtsev, Alexander N.; Frank, Ludmila A.; Kudryavtsev, Alexander; Russian Federation for young scientists [MK-772.2020.4]; Government of Krasnoyarsk Territory, Krasnoyarsk Regional Science Foundation [2021012006966]

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10.

Hydrogen-bond networks between the C-terminus and Arg from the first alpha-helix stabilize photoprotein molecules [Text] / E. V. Eremeeva [et al.] // Photochem. Photobiol. Sci. - 2014. - Vol. 13, Is. 3. - P541-547, DOI 10.1039/c3pp50369k. - 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). . - ISSN 1474-905X. - ISSN 1474-9092

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
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.

WOS
Держатели документа:
[Eremeeva, Elena V.
Burakova, Ludmila P.
Krasitskaya, Vasilisa V.
Kudryavtsev, Alexander N.
Frank, Ludmila A.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Burakova, Ludmila P.
Krasitskaya, Vasilisa V.
Kudryavtsev, Alexander N.
Shimomura, Osamu
Frank, Ludmila A.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Burakova, L.P.; Krasitskaya, V.V.; Kudryavtsev, A.N.; Shimomura, O...; Frank, L.A.; RFBR [12-04-00753-a]; Government of Russian Federation [11.G34.31.0058]

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11.

Dual-analyte single-well bioluminescence immunoassay based on obelin color mutants / A. N. Kudryavtsev, V. V. Krasitskaya, L. A. Frank // Luminescence. - 2012. - Vol. 27, Is. 2. - P131-132. - Cited References: 2 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
[Kudryavtsev, A. N.
Krasitskaya, V. V.
Frank, L. A.] Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia
[Kudryavtsev, A. N.
Krasitskaya, V. V.
Frank, L. A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Kudryavtsev, A.N.; Krasitskaya, V.V.; Frank, L.A.

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12.

Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay [Text] / L. A. Frank, A. I. Petunin, E. S. Vysotski // Russ. J. Bioorg. Chem. - 2004. - Vol. 30, Is. 4. - P. 327-331, DOI 10.1023/B:RUBI.0000037257.80835.7a. - Cited References: 16 . - ISSN 1068-1620

РУБ Biochemistry & Molecular Biology + Chemistry, Organic
Рубрики:
ESCHERICHIA-COLI
   PURIFICATION
   AEQUORIN
   PROTEIN
   CDNA
Кл.слова (ненормированные):
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
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
DIAS Ltd, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Petunin, A.I.; Vysotski, E.S.

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13.

Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay [Text] / L. A. Frank, A. I. Petunin, E. S. Vysotski // Russ. J. Bioorg. Chem. - 2004. - Vol. 30, Is. 4. - P327-331, DOI 10.1023/B:RUBI.0000037257.80835.7a. - Cited References: 16 . - ISSN 1068-1620

РУБ Biochemistry & Molecular Biology + Chemistry, Organic
Рубрики:
ESCHERICHIA-COLI
   PURIFICATION
   AEQUORIN
   PROTEIN
   CDNA
Кл.слова (ненормированные):
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).

Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
DIAS Ltd, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Petunin, A.I.; Vysotski, E.S.

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14.

Calcium-regulated photoproteins of marine coelenterates [Text] / E. S. Vysotski, S. V. Markova, L. A. Frank // Mol. Biol. - 2006. - Vol. 40, Is. 3. - P355-367, DOI 10.1134/S0026893306030022. - Cited References: 99 . - ISSN 0026-8933

РУБ Biochemistry & Molecular Biology
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
Кл.слова (ненормированные):
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.

Держатели документа:
Russian Acad Sci, Siberian Div, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Markova, S.V.; Frank, L.A.

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15.

Calcium-regulated photoprotein obelin as a label in immunoassay: An outlook for applications [Text] / L. A. Frank, V. V. Borisova, E. . Vysotski ; ed. A Tsuji [et al.] // 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). - P. 463-466, DOI 10.1142/9789812702203_0110. - Cited References: 7 . - ISBN 981-256-118-8

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Applied + Chemistry, Physical + Optics
Рубрики:
BIOLUMINESCENT IMMUNOASSAY

WOS
Держатели документа:
RAS, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Borisova, V.V.; Vysotski, E...; Tsuji, A \ed.\; Matsurnoto, M \ed.\; Maeda, M \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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16.

Ca2+-triggered coelenterazine-binding protein from Renilla as an enzyme-dependent label for binding assay [Text] / V. V. Krasitskaya [et al.] // Anal. Bioanal. Chem. - 2011. - Vol. 401, Is. 8. - P2573-2579, DOI 10.1007/s00216-011-5343-2. - 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. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
BIOLUMINESCENT IMMUNOASSAY
   LUCIFERASE
   PURIFICATION
   RENIFORMIS
   MUELLERI
   OBELIN
   PHOTOPROTEIN
   EXPRESSION
   SUBSTRATE
   CLONING
Кл.слова (ненормированные):
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.

Держатели документа:
[Korneeva, S. I.
Kudryavtsev, A. N.
Frank, L. A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Krasitskaya, V. V.
Markova, S. V.
Stepanyuk, G. A.
Frank, L. A.] Russian Acad Sci SB, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Krasitskaya, V.V.; Korneeva, S.I.; Kudryavtsev, A.N.; Markova, S.V.; Stepanyuk, G.A.; Frank, L.A.

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17.

Ca2+-Regulated Photoproteins: Effective Immunoassay Reporters [Text] / L. A. Frank // Sensors. - 2010. - Vol. 10, Is. 12. - P11287-11300, DOI 10.3390/s101211287. - Cited References: 70. - This work was supported by the grant No. 76 of the Russian Academy of Sciences, Siberian Branch. . - ISSN 1424-8220

РУБ Chemistry, Analytical + Electrochemistry + Instruments & Instrumentation
Рубрики:
POLYMERASE-CHAIN-REACTION
   CYTOKINE MESSENGER-RNA
   BIOLUMINESCENT IMMUNOASSAY
   MYCOBACTERIUM-TUBERCULOSIS
   BIOTINYLATED AEQUORIN
   RECOMBINANT AEQUORIN
   ANGSTROM RESOLUTION
   FUSION PROTEIN
   PCR ASSAY
   OBELIN
Кл.слова (ненормированные):
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.

Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.

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18.

Bioluminescent signal system: bioluminescence immunoassay of pathogenic organisms [Text] / L. . Frank [et al.] // Luminescence. - 2007. - Vol. 22, Is. 3. - P215-220, DOI 10.1002/bio.952. - Cited References: 14 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology
Рубрики:
AEQUORIN
   AGENTS
   OBELIN
   ASSAYS
   LABEL
Кл.слова (ненормированные):
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.

Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L...; Markova, S...; Remmel, N...; Vysotski, E...; Gitelson, I...

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19.

Bioluminescent immunoassay of thyrotropin and thyroxine using obelin as a label [Text] / L. A. Frank, A. I. Petunin, E. S. Vysotski // Anal. Biochem. - 2004. - Vol. 325, Is. 2. - P240-246, DOI 10.1016/j.ab.2003.11.003. - Cited References: 16 . - ISSN 0003-2697

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Analytical
Рубрики:
AEQUORIN
   PURIFICATION
   PROTEIN
   CDNA
Кл.слова (ненормированные):
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.

Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
DIAS Ltd, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Petunin, A.I.; Vysotski, E.S.

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20.

Bioluminescent immunoassay of alphafetoprotein with Ca2+-activated photoprotein obelin [Text] / L. A. Frank, E. S. Vysotski ; ed.: JW Hastings, LJ Kricka, J Kricka, // BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS : JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - P439-442. - Cited References: 0 . - 4. - ISBN 0-471-97502-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Frank, L.A.; Vysotski, E.S.; Hastings, JW \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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