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- W2013125587 abstract "Membranes of the lutoids present in the latex of Hevea brasiliensis possess an ATPase which is separable from adsorbed residual acid phosphatase. The pH optimum of the ATPase is 7.75 in Tris—HCl and is displaced to 6.5 in K-phosphate buffer. A divalent cation is obligatory (Mg Mn > Ca). ATP-Mg is the natural substrate of the enzyme. Monovalent cations have practically no action on the enzyme. It is, however, activated by anions, both inorganic (Cl−, HCO3−) and organic (malate, aspartate, tartrate). The enzyme has a higher specificity for ATP than for GTP, CTP or UTP and is non-competitively inhibited by ADP. The enzyme is temperature sensitive and a break in the Arrhenius plot occurs at about 20°, characteristic of membrane-bound enzymes. SH-group poisons inhibit enzyme activity as do classical uncouplers at high concentrations (about 10−3 M). A hypothesis is formulated whereby the membrane-bound lutoid ATPase functions as a proton pump in order to maintain the acid pH of a vacuolar and lysosomal compartment." @default.
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- W2013125587 date "1977-01-01" @default.
- W2013125587 modified "2023-09-25" @default.
- W2013125587 title "ATPase membranaire de vacuoles lysosomales: Les lutoides du latex d'Hevea brasiliensis" @default.
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- W2013125587 doi "https://doi.org/10.1016/0031-9422(77)80088-5" @default.
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