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ENZYMES ENTRAPPED INTO REVERSED MICELLES IN ORGANIC-SOLVENTS - SEDIMENTATION ANALYSIS OF THE PROTEIN-AEROSOL OT-H2O-OCTANE SYSTEMстатья
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: LEVASHOV AV, KHMELNITSKY YL, KLYACHKO NL, CHERNYAK VY, MARTINEK K.
- Журнал: Journal of Colloid and Interface Science
- Том: 88
- Номер: 2
- Год издания: 1982
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 444
- Последняя страница: 457
- DOI: 10.1016/0021-9797(82)90273-9
- Аннотация: Ultracentrifugation was used to study the systems of reversed Aerosol OT micelles in octane that contain solubilized protein (О±-chymotrypsin, lysozyme, trypsin, egg albumin, horse liver alcohol dehydrogenase, Оі-globulin). Changes in the sedimentation coefficients of reversed micelles upon protein entrapment into the latter were found to correlate solely with the molecular weight of solubilized protein in a wide range of experimental conditions, such as the surfactant hydration degree or protein concentration. Proceeding from this, a simple model of solubilization was suggested according to which a protein molecule is entrapped into a reversed micelle in a stoichiometric ratio of 1:1 rendering therewith no significant effect on the size of the reversed micelle. The conditions were found by the example of О±-chymotrypsin under which the sedimentation properties of the system deviate from those of the model. The deviations occur at rather low hydration degrees of the surfactant when the inner cavity of a reversed micelle is less than the effective size of the solubilized protein molecule. In the latter cause the protein "creates" around itself a new micelle of a required (bigger) size
- Добавил в систему: Клячко Наталья Львовна