Abstract
1. 1. The substrate kinetics of the enolase reaction has been investigated with Mg ++, Mn ++, and Zn ++ as activating ions. No differences in the affinities of the three metallo-enzymes for the substrate could be detected. 2. 2. The interaction of bovine serum albumin with dl-2-phosphoglyceric acid has been studied with and without added Zn ++. It was shown that Zn ++ can act as a mediator in the binding of the acid to the protein. 3. 3. The interaction of purified enolase with its substrates has been studied with and without added Mg ++ or Zn ++. It was found that the substrates are bound to the enzyme also in the absence of metal ions.
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