Characterization of the solubilized plasma membrane ATPase of red beet

The p1mm membrane ATP-phosphohydrolm (ATPae) frm red beet (Bta swirb L) storge tissue wasol d ith the zwitterionic eter t Zittergea 3-14 from a plas membne-enriched fion which e with the aok det t, sodium deoxycholate. For both the extraction of ext s pe by deoxycholate awl the soublo t of active plasm membrane ATPase by Zw tteg 3-14, the op l co rtin ofd nt was 0.1% (weigt per vome) with a dett to protein ratio of 1.0(per). The of the solublUzed ATPase were fonnd to be similar to the mebrane-bomd enyme wit respect to pH oium, subtrate specificity, ibitor sensitivity, an kietics of K⁺ stimulation. The solubiHzed ATPase pretio formed a rapidly uring over phospbheyme, the bradW veloiy of whic wa as in the presene of 50 millimolr KC. So2b Mtonwith 0.1% Zwtergent 3-14 fohowig extation with 0.1% deoxycolate resulted in an inem in both ATPae activity and steady sate pbospboenzyne level; however, a direct correspnee betwee the increas in ATPase tivity and pLhospborylatio lvel did nt exist. It Is that this diepacy may be the result of a deternt-m ated m ctIon of kinetic rate consats in the mechanism of the enzyme.