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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) : Purtov K.V., Petunin A.I., Burov A.E., Puzyr A.P., Bondar V.S.
Заглавие : Nanodiamonds as Carriers for Address Delivery of Biologically Active Substances
Колич.характеристики :6 с
Коллективы :
Место публикации : Nanoscale Res. Lett.: SPRINGER, 2010. - Vol. 5, Is. 3. - С. 631-636. - ISSN 1931-7573, DOI 10.1007/s11671-010-9526-0
Примечания : Cited References: 24. - This work was supported by the Program # 27 for Basic Research of the Presidium of RAS (project 3.6.3).
Предметные рубрики: ANTICANCER DRUGS
NANOPARTICLES
ADSORPTION
PARTICLES
PROTEINS
Ключевые слова (''Своб.индексиров.''): nanodiamonds--ligand--protein immobilization--nanocarrier--targeted delivery
Аннотация: Surface of detonation nanodiamonds was functionalized for the covalent attachment of immunoglobulin, and simultaneously bovine serum albumin and Rabbit Anti-Mouse Antibody. The nanodiamond-IgG(I125) and RAM-nanodiamond-BSA(I125) complexes are stable in blood serum and the immobilized proteins retain their biological activity. It was shown that the RAM-nanodiamond-BSA(I125) complex is able to bind to the target antigen immobilized on the Sepharose 6B matrix through antibody-antigen interaction. The idea can be extended to use nanodiamonds as carriers for delivery of bioactive substances (i.e., drugs) to various targets in vivo.
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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) : Krasitskaya V. V., Bashmakova E. E., Kudryavtsev A. N., Vorobjeva M. A., Shatunova E. A., Frank L. A.
Заглавие : The Hybrid Protein ZZ-OL as an Analytical Tool for Biotechnology Research
Колич.характеристики :7 с
Коллективы : Russian FederationRussian Federation [MK-772.2020.4]; Russian Science FoundationRussian Science Foundation (RSF) [16-14-10296]
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2020. - Vol. 46, Is. 6. - С. 1004-1010. - ISSN 1068-1620, DOI 10.1134/S106816202006014X. - ISSN 1608-330X(eISSN)
Примечания : Cited References:14. - The study 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 in the part involving the synthesis and analysis of variants of proteins with melanoma-inhibiting activity) and a grant of the Russian Science Foundation (project no. 16-14-10296 in the part involving the bioluminescence analysis of binding of DNA aptamers to targets).
Аннотация: The gene of the hybrid protein that encodes the double synthetic fragment proZZ of the immunoglobulin-binding domain of protein A of Staphylococcus aureus and apo-obelin joined by a short linker has been cloned. The corresponding hybrid protein has been obtained by expression in Escherichia coli cells. The protein activated with a substrate (coelenterazine) possesses the bioluminescent Ca2+-dependent activity of the photoprotein close to that of recombinant wild-type obelin, and the immunoglobulin-binding ability of protein A. It has been shown that the hybrid can be used as a highly sensitive label to detect antibodies and estimate their affinity and interaction with recombinant proteins, as well as in investigations of other kinds.
WOS
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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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