Thiamine triphosphatase activity in bovine kidney

Properties of soluble thiamine triphosphatase (ThTPase), adenosine triphosphatase, nucleoside triphosphatase and alkaline phosphatase activities in bovine kidney were compared. ThTPase and the other phosphatases differed clearly in their pH‐dependences, Km and molecular masses. Apparent Km and pH op...

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Veröffentlicht in:	Biochemistry and molecular biology international 1998-09, Vol.46 (1), p.115-123
Hauptverfasser:	Makarchikov, Alexander F., Chernikevich, Ivan P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid Anhydride Hydrolases - metabolism Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Alkaline Phosphatase - metabolism Animals Bovine kidney Cattle Chromatography, Gel Hydrogen-Ion Concentration Inosine Triphosphate - metabolism Kidney - enzymology Kinetics Molecular Weight Nucleoside-Triphosphatase Thiamin-Triphosphatase - chemistry Thiamin-Triphosphatase - metabolism thiamine triphosphatase Thiamine Triphosphate - metabolism
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Zusammenfassung:	Properties of soluble thiamine triphosphatase (ThTPase), adenosine triphosphatase, nucleoside triphosphatase and alkaline phosphatase activities in bovine kidney were compared. ThTPase and the other phosphatases differed clearly in their pH‐dependences, Km and molecular masses. Apparent Km and pH optimum for ThTPase were determined to be 45.5 μM and 8.9, respectively. Molecular mass of the enzyme was 29.1 kDa as estimated by Sephadex G‐100 gel filtration. The results obtained show bovine kidney to contain a specific soluble ThTPase, this enzyme being the only one hydrolyzing low concentrations of ThTP.
ISSN:	1521-6543 1039-9712 1521-6551
DOI:	10.1080/15216549800203622