|
ИСТИНА |
Войти в систему Регистрация |
ИПМех РАН |
||
ARTIFICIALLY GLYCOSYLATED ALPHA-CHYMOTRYPSIN IN REVERSED MICELLES OF AEROSOL OT IN OCTANE - A NEW APPROACH TO ELUCIDATION OF THE ROLE OF CARBOHYDRATE MOIETIES IN GLYCOPROTEINSстатья
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: LEVASHOV AV, RARIY RV, MARTINEK K., KLYACHKO NL
- Журнал: FEBS Letters
- Том: 336
- Номер: 3
- Год издания: 1993
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 385
- Последняя страница: 388
- DOI: 10.1016/0014-5793(93)80842-I
- Аннотация: A comparative study of native and artificially glycosylated alpha-chymotrypsin in reversed micelles of Aerosol OT in octane was carried out. D-Glucosamine and 1-ethyl-3-(3-dimethylaminopropyr)carbodiimide were used as modifying agents to yield glycosylated enzyme. Unlike the native alpha-chymotrypsin, the modified protein tended to form reversible oligomeric structures, revealed by the appearance of an additional maximum (characteristic of dimeric forms of protein functioning) as a result of the enzyme catalytic activity being dependent on the AOT hydration degree. Dependence of the enzyme catalytic activity on the surfactant concentration in the case of the modified enzyme was similar to that of glycoproteins, and suggests its membrane affinity. The role of carbohydrate moieties in the functioning of glycoproteins is discussed.
- Добавил в систему: Клячко Наталья Львовна