Über die Quecksilber-Aktivierung der Glycerinsäure-2.3-diphosphatase

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Abstract
The enzyme, obtained from rabbit muscle, hydrolyzes 2,3-diphosphoglyceric acid to 3-phosphoglyceric acid. The latter compound inhibited, whereas 2-phosphoglyceric acid activated. Hg++ ions activated in a narrow concentration range between 0.07 m[image]to 0.2 m[image]; higher concentrations inhibited. Ag+ ions activated in the same concentration range, but not as much. Cu++ inhibited. The specificity of the enzyme both in the presence and absence of Hg++ and 2-phosphoglyceric acid was investigated; it appeared to be absolute. The Michaelis constant KM and the pH optimum were determined. It was found that Hg++ only activated in the presence of compounds containing N; presumably the activator was a complex between Hg and these compounds.

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