|
ИСТИНА |
Войти в систему Регистрация |
ФНКЦ РР |
||
Fusion proteins based on firefly luciferase and their application in biospecific assaysтезисы доклада
- Авторы: Smirnova D.V., Ugarova N.N.
- Сборник: Abstracts of International Conference Biocatalysis-2017: Fundamentals & Applications, June 25-30, 2017, Moscow Region, Russian Federation
- Тезисы
- Год издания: 2017
- Место издания: ООО «Иннотех МГУ Москва
- Первая страница: 93
- Последняя страница: 94
- Аннотация: Firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutants the enzyme with prescribed spectral characteristics, and abundance of bacterial expression systems suitable for large-scale production of recombinant proteins. Firefly luciferase has absolute specifity to its substrates: luciferin and ATP. Based on this unique property, there are many methods for detection of analytes involved into the process of formation or degradation of ATP The choice of protein domains is limited by both their properties and availability of the expression system suitable for production of luciferase-based fusion proteins. That is why it is common to produce fusion proteins of luciferase with universal protein domains specific to a the entire class of compounds such as Protein А [1], Protein G [2], and DNA-binding domain [3]. Streptavidin-luciferases [4, 5] and biotin-luciferases [6] are in particular interest due to their ability to fix the luciferase molecule on the surface of a target via highly specific biotin-streptavidin interactions.
- Добавил в систему: Угарова Наталья Николаевна