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Membrane Particles, Proteins and ATPase Activity of Tonoplast Vesicles of Mesembryanthemum crystallinum in the C‐3 and CAM State *
Author(s) -
Klink R.,
Haschke H.P.,
Kramer D.,
Lüttge U.
Publication year - 1990
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.1438-8677.1990.tb00121.x
Subject(s) - mesembryanthemum crystallinum , vacuole , atpase , vesicle , crassulacean acid metabolism , v atpase , biochemistry , biology , membrane , chemistry , biophysics , enzyme , photosynthesis , cytoplasm
Dimensions and area densities of membrane particles were studied by electron microscopy of replicas of freeze‐fractured suspensions of tonoplast vesicles of Mesembryanthemum crystallinum L. in the C‐3 state and after induction of crassulacean acid metabolism (CAM) by salinity. The results are compared with the relative contribution of tonoplast‐ATPase protein to total membrane protein obtained from integration of elution profiles in size‐exclusion chromatography. Coverage of tonoplast area by globular membrane particles was 20% and 36 % and ATPase in relation to total membrane protein was 33 % and 35 % in C‐3 and CAM M. crystallinum , respectively. Thus, by order of magnitude, it is most likely that the particles represent the ATPase. In Kalanchoë daigremontiana Hamet et Perrier de la Bâthie the ATPase also constituted 36% of total tonoplast protein. Induction of CAM in M. crystallinum was associated with an increase in specific ATPase activity of the tonoplast and an increase of the size and area coverage of tonoplast particles, whereas the relative contribution of ATPase protein to total tonoplast protein and the molecular mass of the ATPase holoenzyme, as seen in size‐exclusion chromatography, remained almost unchanged.