Abstract
A newly developed AMP selective enzyme electrode has been used to make direct binding measurements of the allosteric interaction between AMP and D-fructose-1,6-diphosphatase (E.C. No. 3.1.3.11). The proposed technique is based upon the ability of the enzyme electrode to distinguish between free and bound nucleotide. D-fructose-1,6-diphosphatase from rabbit muscle was found to have four binding sites for AMP with an average binding constant of 9 × 10 4 M −1. The advantages of a direct electrode method for determining nucleotide binding constants are discussed.
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