Solubilization, purification, and characterization of the ATPase from spinach leaves plasma membrane fraction and its sensitivity to herbicides [electronic resource].

Includes references.

The plasma membrane ATPase of spinach leaves (Spinacia oleracea) bad been solubilized with a two-step procedure using the anionic detergent, deoxycbolate (DOC) and the non ionic detergent, aminoxid WS35 as follows: I) loosely bound membrane proteins are removed by treatment with 0.1% DOC; 2) The ATPase is solubilized with 0.1 % aminoxid WS35 in the presence of 1 % DOC; 3) the solubilized material is further purified by centrifugation through a glycerol gradient (45-70%). Typically, about 10% of the ATPase activity is recovered, and the specific activity increases about II-fold. The properties of the purified ATPase are essentially the same as those of membrane-bound ATPase, with respect to substrate specificity, inhibitor sensitivity, and ion stimulation.

Summary in Arabic.

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