| Literature DB >> 6220703 |
G Parenti Castelli, A Baracca, R Fato, A Rabbi.
Abstract
The temperature dependence of the intrinsic tryptophan fluorescence in either bovine heart submitochondrial particles or oligomycin-sensitive ATPase isolated therefrom shows a discontinuity at near 25 degrees C, which coincides with the temperature where a break in the Arrhenius plot of ATPase activity is found. Addition of n-butanol to submitochondrial particles induces a decrease of tryptophan fluorescence in the whole temperature range. The discontinuity is interpreted as a temperature-dependent structural change and related to a viscosity-induced phase separation of the intrinsic mitochondrial proteins.Entities:
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Year: 1983 PMID： 6220703 DOI： 10.1016/0006-291x(83)90315-7
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575