Abstract
Binding of Sr2+ to bean mitochondria (Phaseolus vulgaris) shows a dissociation constant of 25 × 10−6 and results in 40 to 50 nmoles of Sr2+ bound per mg protein. The binding is partially inhibited by valinomycin plus K+, 2, 4-dinitrophenol, as well as ruthenium red at a level of the 120 nmoles per mg protein. These compounds also partially inhibit active uptake of Sr2+. Calcium and Mg2+ also partially inhibit binding in the same magnitude as previously reported for inhibition of transport. Phosphate which is required for divalent cation transport is without effect on the binding of Sr2+. The possible role of the observed binding sites in divalent cation transport is discussed.
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