Temperature-Dependent Conformation Changes Of Ribulose-1,5-Bisphosphate Carboxylase Studied By Use Of 1-Anilino-8-Naphthalene Sulfonate
Zeitschrift für Naturforschung C(1977)
Abstract
Abstract The influence of temperature on the structure and enzyme activity of ribulose-1,5-bisphosphate carboxylase, isolated from Euglena gracilis cells, was studied. Freezing of the purified ribulose-1,5-bisphosphate carboxylase preparation causes a severe loss of enzyme activity, which can be restored again by incubation of the enzyme molecules at higher temperatures (50 °C). The titration of both enzyme samples with the fluorescence probe 1-anilino-8-naphthalene sulfonate (ANS) revealed an increase of the fluorescence emission of the low temperature form of the enzyme. Two different enzyme conformations can be assumed which differ in the number of binding sites for ANS and Vmax values for the carboxylase reaction but show similar binding constants for ANS and the apparent Km values for C02 .
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Key words
temperature dependent conformation changes
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