Purification and properties of trehalase from monkey small intestine.

ABSTRACT

Brush border membrane trehalase was purified from monkey small intestine by a procedure which includes solubilisation by Triton X-100, ammonium sulphate fractionation, and chromatography on DE-52 and hydroxyapatite. The purified enzyme had a specific activity of 11 units/mg protein and was purified 140-fold. The enzyme showed a single protein band on Polyacrylamide gel electrophoresis. It had a Km value of 17·4 mM for trehalose and a Vmax of 1·33 units. Sucrose and Tris acted as competitive inhibitors of the enzyme.