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Solubilization and Functional Reconstitution of the Tonoplast H +-ATPase from Citrus in Liposomes

Bañuls, Josefina ; Ratajczak, Rafael ; Lüttge, Ulrich

Journal of plant physiology, 1994, Vol.144 (1), p.74-79 [Periódico revisado por pares]

Elsevier GmbH

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  • Título:
    Solubilization and Functional Reconstitution of the Tonoplast H +-ATPase from Citrus in Liposomes
  • Autor: Bañuls, Josefina ; Ratajczak, Rafael ; Lüttge, Ulrich
  • Assuntos: ADENOSINA TRIFOSFATASA ; ADENOSINE TRIPHOSPHATASE ; Adenosintriphosphatase ; Blatt ; CELL MEMBRANES ; CITRUS SINENSIS ; Citrus sinensis (L) ; CYTOPLASMIC ORGANELLES ; FEUILLE ; H +-ATPase ; HOJAS ; LEAVES ; Liposom ; MEMBRANAS CELULARES ; MEMBRANE CELLULAIRE ; Orange ; ORGANITE CELLULAIRE ; ORGANULOS CITOPLASMICOS ; Protein ; PROTEINAS ; PROTEINE ; PROTEINS ; reconstitution ; Tonoplast
  • É parte de: Journal of plant physiology, 1994, Vol.144 (1), p.74-79
  • Notas: F60
    94G0881
  • Descrição: Proteoliposomes were formed after solubilization of tonoplast proteins from Citrus with octylglucoside in the presence of soybean phospholipids (phosphatidylcholine), with removal of detergent by passage through an Amberlite XAD-2 column. The specific ATP-hydrolysis activity of the proteoliposomes was increased 4-fold over the activity of the native tonoplast vesicles. Pumping of protons by the reconstituted ATPase was demonstrated by quinacrine-fluorescence quenching. Neither vanadate nor azide inhibited ATP-hydrolysis and transport activity. Both the ATP-hydrolysis and the H +-translocating activities were inhibited by nitrate, the first activity being the more sensitive one. Both activities were completely inhibited by bafilomycin A 1, an inhibitor of vacuolar type ATPase, at concentrations of 20 nM. A potent inhibitor of H +-transport, DCCD, completely inhibited both activities at 100 gM and with halfmaximal inhibition at concentrations of 40 pM and 60 μM for the H +-transport and the ATP-hydrolysis activities, respectively. The reconstituted H+-ATPase was stimulated by anions (Cl - > Br - > SO 4 2−), inhibited by NO 3 − and I − and largely insensitive to monovalent cations. The proteoliposomes showed no PP iase activity. SDS-PAGE showed that the reconstituted H +-ATPase from Citrus contained polypeptides of apparent molecular masses of 63, 52, 37, 33 and 16 kDa that cross-reacted with an antiserum against the tonoplast ATPase from Kalanchoë daigremontiana. Freeze-fracture electron microscopy of the proteoliposomes showed that proteins were incorporated into the bilayer membrane. The proteoliposomes from Citrus were mainly vesicles intramembraneous with particles whose diameter ranged from 6 to 7 nm. The results conclusively demonstrate a selective reconstitution of a functional H +-ATPase from Citrus.
  • Editor: Elsevier GmbH
  • Idioma: Inglês
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