The Inactivation of Sheep Liver Sorbitol Dehydrogenase by Pyrophosphate and Some Analogous Metal Chelators

• Published in: Archives of biochemistry and biophysics Vol. 311; no. 2; pp. 450 - 456
• Main Authors: Reiersen, H., Lindstad, R.I., Mckinleymckee, J.S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.06.1994
• Subjects: Animals; chelateur; chelating agents; Chelating Agents - pharmacology; cinc; Diphosphates - pharmacology; Enzyme Activation; foie; higado; Kinetics; L-Iditol 2-Dehydrogenase - antagonists & inhibitors; L-Iditol 2-Dehydrogenase - metabolism; liver; Liver - enzymology; Molecular Structure; ovin; ovinos; oxidoreductases; oxidorreductasas; oxydoreductase; pirofosfatos; Polyphosphates - pharmacology; pyrophosphate; pyrophosphates; quelatos; Sheep; Structure-Activity Relationship; zinc; Zinc - pharmacology

Pyrophosphate and several other metal chelators are shown to inactivate sheep liver sorbitol dehydrogenase. Pyrophosphate, tripolyphosphate, and some bisphosphonates inactivate the enzyme by saturation kinetics involving the formation of a reversible complex. A mechanism for the pyrophosphate-mediat...