Thiamine Triphosphatase from Electrophorus Electric Organ Is Anion-Dependent and Irreversibly Inhibited by 4,4'-Diisothiocyanostilbene-2,2'disulfonic Acid
Bettendorff, Lucien; Wins, Pierre; Schoffeniels, Ernest
1988 • In Biochemical and Biophysical Research Communications, 154 (3), p. 942-947
[en] Thiamine triphosphatase (TTPase) from membranes isolated from the main electric organ of E. electricus is activated about 8 fold by NO3-, I- and SCN- while SO42- is inhibitory. Activating anions shift the pH optimum of the enzyme from 5.0 to 8.0. The enzyme is irreversibly inactivated by low concentrations of 4,4'-diisothiocyano-2,2' disulfonic acid (DIDS), an inhibitor of anion transport. Anions protect from DIDS inactivation. These and other results suggest that the membrane-bound TTPase activity is tightly controlled, possibly through mechanisms involving anion transport.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bettendorff, Lucien ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique
Wins, Pierre
Schoffeniels, Ernest
Language :
English
Title :
Thiamine Triphosphatase from Electrophorus Electric Organ Is Anion-Dependent and Irreversibly Inhibited by 4,4'-Diisothiocyanostilbene-2,2'disulfonic Acid
Publication date :
1988
Journal title :
Biochemical and Biophysical Research Communications
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