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ARTIFICIAL OLIGOMERIZATION OF ENZYMES - A NEW APPROACH TO THE CATALYTIC ACTIVITY REGULATION IN REVERSED MICELLESстатья
Информация о цитировании статьи получена из
Scopus,
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: NAMETKIN SN, KABANOV AV, KLYACHKO NL, LEVASHOV AV
- Журнал: Bioorganicheskaya Khimiya
- Том: 17
- Номер: 6
- Год издания: 1991
- Издательство: Izdatel'stva Nauka
- Местоположение издательства: Russian Federation
- Первая страница: 756
- Последняя страница: 759
- Аннотация: Comparative studies were carried out in the catalytic activity regulation of native alpha-chymotrypsin and its artificially produced hexameric form as an example of non-disociating oligomeric enzyme (covalently cross-linked by means of succinimidyl-3-(2-pyridylthiopropionate)) in the Aerosol OT reversed micelles in octane. Native (monomeric) alpha-chymotrypsin exhibits maximal catalytic activity in the reversed micelles at the hydration degree w0 = 10, when the radius of the micelle inner cavity is equal to the radius of the alpha-chymotrypsin globule. For the alpha-chymotrypsin hexamer, optimun is observed at w0 = 45, with the inner micellar cavity radius (r = 68 angstrom) being approximately equal to the radius of the sphere surrounding the octahedral combination of the six monomeric alpha-chymotrypsin molecules (r = 61 angstrom). Thus, construction of the corresponding oligomeric structures is made easy, with the optimal catalytic activity in a preset range of the hydration degrees.
- Добавил в систему: Клячко Наталья Львовна