Idioma:

Separation and purification of the tonoplast ATPase and pyrophosphatase from plants with constitutive and inducible Crassulacean acid metabolism

Bremberger, C. ; Haschke, H.-P. ; Lüttge, U.

Planta, 1988-10, Vol.175 (4), p.465-470 [Periódico revisado por pares]

Berlin: Springer-Verlag

Texto completo disponível

Citações Citado por

Enviar para

Título:
Separation and purification of the tonoplast ATPase and pyrophosphatase from plants with constitutive and inducible Crassulacean acid metabolism
Autor: Bremberger, C. ; Haschke, H.-P. ; Lüttge, U.
Assuntos: Adenosine triphosphatases ; adenosinetriphosphatase ; Biological and medical sciences ; Cell biochemistry ; Cell physiology ; Chromatography ; Crassulacean acid metabolism ; Elution ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gels ; Kalanchoe daigremontiana ; Mandalas ; Mesembryanthemum crystallinum ; Molecular weight ; Plant physiology and development ; Plants ; pyrophosphatase ; Tonoplast ; tonoplasts
É parte de: Planta, 1988-10, Vol.175 (4), p.465-470
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Tonoplast vesicles were isolated from Kalanchoe daigremontiana Hamet et Pierrer de la Bâthie and Mesembryanthemum crystallinum L., exhibiting constitutive and inducible crassulacean acid metabolism (CAM), respectively. Membrane-bound proteins were detergent-solubilized with 2% of Triton X-100. During CAM induction in M. crystallinum, ATPase activity increases four-fold, whereas pyrophosphatase activity decreases somewhat. With all plants, ATPase and pyrophosphatase could be separated by size-exclusion chromatography (SEC, Sephacryl S 400), and the ATPase was further purified by diethylaminoethyl-ion-exchange chromatography. Sodium-dodecyl-sulfate electrophoresis of the SEC fractions from K. daigremontiana containing maximum ATPase activity separates several protein bands, indicating subunits of 72, 56, 48, 42, 28, and 16 kDa. Purified ATPase from M. crystallinum in the C3 and CAM states shows a somewhat different protein pattern. With M. crystallinum, an increase in ATP-hydrolysis and changes in the subunit composition of the native enzyme indicate that the change from the C3 to the CAM state is accompanied by de-novo synthesis and by structural changes of the tonoplast ATPase.
Editor: Berlin: Springer-Verlag
Idioma: Inglês

Links

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Separation and purification of the tonoplast ATPase and pyrophosphatase from plants with constitutive and inducible Crassulacean acid metabolism

Bremberger, C. ; Haschke, H.-P. ; Lüttge, U.

Berlin: Springer-Verlag

Buscando em bases de dados remotas. Favor aguardar.