Ribulose-1,5-bisphosphate carboxylase from plants adapted to extreme environments
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概要
- 論文の詳細を見る
The K_m and V_<max> of ribulose- 1,5-bisphosphate carboxylase (RuBPCase) in selenium absorbing plants (Astragalus flavus Barn., Astragalus rafaelensis Barn. and Stanleya pinnata Bril.) were similar to RuBPCase from tomato (Lycopersicon esculentum L. var. tropic). The pH optima for RuBPCase activity was 8.0 for L. esculentum and A. flavus and 7.0 for A. rafaelensis and S, pinnata. The Activation Energy (ΔE) values for the enzymes were as follows: A. flavus (21.37), S. pinnata (19.85), A. rafaelensis (19.12) and L. esculentum (18.58). The energy of activation was higher for the desert plants as compared to the tomato. The Arrhenius plot curves were linear to 50℃ for the desert plants as compared to 45℃ for tomato. Enzyme kinetics of RuBPCase from halophytic plants (Salicornia paclfica Stand., var. utahensis (Tidestrom) Munz, and Salicornia rubra Nels.) indicated the enzyme was at least as sensitive to NaCl concentrations as the enzyme from tomato.
- 日本植物生理学会の論文
著者
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Hess Samuel
Department Of Botany And Range Science Brigham Young University
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Weber D.J.
Department of Botany and Range Science,Brigham Young University
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Andersen William
Department of Botany and Range Science,Brigham Young University
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Hansen D.J.
Department of Botany and Range Science,Brigham Young University
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Gunasekaran M.
Department of Botany and Range Science,Brigham Young University
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Gunasekaran M.
Department Of Botany And Range Science Brigham Young University
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Hansen D.j.
Department Of Botany And Range Science Brigham Young University
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Andersen William
Department Of Botany And Range Science Brigham Young University
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Weber D.j.
Department Of Botany And Range Science Brigham Young University