Acid Phosphatase from Rat Liver
نویسنده
چکیده
Rat liver acid phosphatase (EC 3.1.3.2) was separated into two highly purified fractions, differing in isoelectric point and Km. One fraction was crystallized and proved homogeneous by ultracentrifugation and polyacrylamide gel electrophoresis. The molecular weights (lOO,OOO), substrate specificities, and pH optima of both enzymes were similar. Oxalate was a mixed type inhibitor to both enzymes. In the presence of dioxane, both enzymes exhibited sigmoidal inhibition curves by oxalate and by trypan blue.
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تاریخ انتشار 2003