Thiamine triphosphatase activity in bovine kidney.

Abstract

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, K(m) and molecular masses. Apparent K(m) and pH optimum for ThTPase were determined to be 45.5 microM 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.