Purification and properties of trehalase from monkey small intestine.
J Biosci
;
1988 Jun; 13(2): 153-158
Artículo
en Inglés
| IMSEAR
| ID: sea-160654
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.
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Índice:
IMSEAR (Asia Sudoriental)
Idioma:
Inglés
Revista:
J Biosci
Año:
1988
Tipo del documento:
Artículo
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