Главная
Авторизация
Фамилия
Пароль
 

Базы данных


Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Область поиска
Формат представления найденных документов:
полныйинформационныйкраткий
Отсортировать найденные документы по:
авторузаглавиюгоду изданиятипу документа
Поисковый запрос: (<.>K=proZZ<.>)
Общее количество найденных документов : 2
Показаны документы с 1 по 2
1.


   
    The Hybrid Protein ZZ-OL as an Analytical Tool for Biotechnology Research / V. V. Krasitskaya, E. E. Bashmakova, A. N. Kudryavtsev [et al.] // Russ. J. Bioorg. Chem. - 2020. - Vol. 46, Is. 6. - P1004-1010, DOI 10.1134/S106816202006014X. - 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). . - ISSN 1068-1620. - ISSN 1608-330X
РУБ Biochemistry & Molecular Biology + Chemistry, Organic

Кл.слова (ненормированные):
С -- а -- (2+)-regulated photoprotein obelin -- proZZ -- hybrid -- protein -- IgG -- bioluminescence assay
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
Держатели документа:
Russian Acad Sci, Fed Res Ctr, Krasnoyarsk Res Ctr, Siberian Branch,Inst Biophys, Akad Gorodok 50-50, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia.

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Kudryavtsev, A. N.; Vorobjeva, M. A.; Shatunova, E. A.; Frank, L. A.; Russian FederationRussian Federation [MK-772.2020.4]; Russian Science FoundationRussian Science Foundation (RSF) [16-14-10296]

Найти похожие
2.


   
    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.

Найти похожие
 

Другие библиотеки

© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)