By Felix Bronner, Arnost Kleinzeller (Eds.)
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Extra resources for Current Topics in Membranes and Transport, Vol. 3
Ouabain prevented the chase and the (E-P-32P)-ouabain complex was slowly hydrolyzed leaving a dephospho-(enzyme)-ouabain complex. Thus, it appears that glycosides inhibit the sodium-dependent step in a somewhat indirect manner. Another approach has provided insight into the sodium-potassium effectson glycoside-3H interaction with the system. Membranes containing Na+,K+-ATPase activity which are exposed to [ATP magnesium 4sodium], or t o [magnesium inorganic phosphate] bind ~ u a b a i n - ~ H at relatively slow rates in the presence of potassium (Lindenmayer, 1970; Lindenmayer and Schwartz, 1970b).
It should be emphasized that the protocols of the experiments by Shamoo and Brodsky (1972) and the studies by NGrby and Jensen (1971) are different, but both results suggest an intermediary membrane-ATP complex. Post et al. (1969) reported indirect evidence of an ATP-enzyme complex. , a nonphosphorylating condition). , whichever was lacking) such that incorporation of phosphate was favored. P-32P,as opposed to -31P(nonisotopic), was incorporated into the preparation. This implies that ATP-32P was bound prior to the transphosphorylation reaction.
Heinz and Hoffman (1965), and Ngrby and Jensen in Skou’s laboratory (1971) recently demonstrated binding of ATP to Na+, K+-ATPase preparations. The latter study, using a rapid dialysis rate technique, reported ATP binding of about 2 pmoles per unit activity over a range of enzyme activities. This binding did not require magnesium (or at least the latter was much lower than that required for hydrolysis), and the apparent dissociation constant for the complex was increased b y potassium. Also the binding was independent of sodium.