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LECTIN-LIKE CENTER IN THE MOLECULE OF ALPHA-CHYMOTRYPSIN - FORMATION OF COMPLEXES WITH PEROXIDASE AND ARTIFICIALLY GLYCOSYLATED ALPHA-CHYMOTRYPSINстатья
Информация о цитировании статьи получена из
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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: RARIY RV, KLYACHKO NL, BORISOVA EA, PENAGOS CJC, LEVASHOV AV
- Журнал: Biochemistry and molecular biology international
- Том: 36
- Номер: 1
- Год издания: 1995
- Издательство: Taylor & Francis
- Местоположение издательства: United Kingdom
- Первая страница: 31
- Последняя страница: 37
- Аннотация: Using the system of reversed micelles of Aerosol OT1 in octane as an instrument revealing the possibility of supramolecular structures formation, we have shown that the native alpha-chymotrypsin can form complexes with glycoproteins. Dimers of the native alpha-chymotrypsin with the artificially glycosylated one and with horseradish peroxidase (natural glycoprotein) were obtained. The position of the optimum on the dependence of the catalytic activity upon the hydration degree confirms the compact organization of the formed complexes. The ability of alpha-chymotrypsin to form such kind of complexes seems to play a key role in its absorption on glycocalix in vivo.
- Добавил в систему: Клячко Наталья Львовна