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Biochemical and Immunological Properties of Solubilized Tonoplast ATPase of the Facultative CAM Plant Mesembryanthemum crystallinum in the C 3 and CAM States
Author(s) -
Struve I.,
Lüttge U.
Publication year - 1988
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1988.tb00009.x
Subject(s) - mesembryanthemum crystallinum , atpase , biochemistry , vacuole , crassulacean acid metabolism , atp hydrolysis , kalanchoe , proton transport , v atpase , fusicoccin , chemistry , biology , biophysics , enzyme , membrane , photosynthesis , botany , cytoplasm
A nitrate‐sensitive, azide‐insensitive ATPase isolated from M. crystallinum in the C 3 and in the CAM state has been solubilized in active form using octylglucoside and Zwittergent 3–14. Like the membrane‐bound tonoplast ATPase, the solubilized ATPase showed an increase in ATP‐hydrolysis activity after transition from the C 3 to the CAM mode of photosynthesis. The characteristics of the membrane‐bound and the solubilized tonoplast ATPase were comparable with respect to salt stimulation, inhibitor effects, and MgATP 2– ‐concentration dependence. Differing from the membrane‐bound ATPases, the solubilized ATPase from C 3 ‐ and CAM‐ M. crystallinum showed a pH optimum between pH 6.5 and 7.0. In order to compare the solubilized ATPases immunologically, antibodies were prepared against the tonoplast fraction of C 3 ‐ and CAM‐ M. crystallinum . A cross‐reaction was observed between antibodies against the tonoplast ATPase from C 3 ‐ and CAM‐ M. crystallinum and the solubilized ATPase from C 3 ‐ and CAM‐ M. crystallinum . A cross‐reaction was also observed between antibodies against the tonoplast ATPase from C 3 ‐ and CAM‐ M. crystallinum and the solubilized tonoplast ATPase from Kalanchoë daigremontiana . However, there was no cross‐reaction with the solubilized plasmalemma ATPase from Festuca rubra .