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SPECIFIC EFFECT OF AMMONIUM ION ON THE ENZYME-ACTIVITY OF MYOSIN AND SUBFRAGMENT-Iстатья
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: LOBYSHEV VI, VISHNEVSKAYA ZI
- Журнал: Biophysics
- Том: 37
- Номер: 5
- Год издания: 1992
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 920
- Последняя страница: 922
- Аннотация: The kinetic isotope effect of hydrolysis of ATP by myosin subfragment-I in the presence of K+, NH4+, Rb+ was measured. V(H)/Y(D) was found to be 1.8; 1.3; 2.0, respectively. According to the thermodynamic isotope effect induced by hydration, the kinetic isotope effect must increase with the increase of cation size from K+ to Rb+. The size of ammonium ions is the intermediate between K+ and Rb+, but the observed isotope effect in the presence of ammonium is much lower than in the presence of e and Rb+. The results suggest that monovalent cations occur near the active center of the enzyme and contribute to some extent lo the hydrolysis reaction but the specificity of ammonium ions seems not to be due to its ideal steric accordance. The obtained results support the viewpoint that NH4+ ions as donor of protons participate in the chemical stage of ATP hydrolysis by subfragment-I.
- Добавил в систему: Лобышев Валентин Иванович