Studies on inositolphosphatase in rat small intestine.
The possibility that inositolphosphatase differs from other intestinal phosphatases was tested by comparing several enzymatic characteristics of phosphatase activities of rat intestinal homogenate acting on various specific substrates. Optimum pH and temperature, Km, Vmax, heat stability, inhibition and metal ion requirement studies suggest that inositolphosphatase differs from phytase and p-nitrophenylphosphatase. Furthermore, we found that inositolphosphatase activity was about 2 times higher in duodenum and jejunum than ileum. It sedimented (90-100%) with a high-speed particulate fraction of mucosal homogenate; 42% of the activity was separated with the brush border membrane isolated from mucosal homogenate. Partial separation by gel filtration on Sephadex G200 and chromatography on phenyl Sepharose CL 4B provided additional evidence to suggest that inositolphosphatase and phytase are different enzymes.
D010832:6-Phytase / Q000032:analysis; D000469:Alkaline Phosphatase / Q000032:analysis; D000818:Animals; D006358:Hot Temperature; D006868:Hydrolysis; D007295:Inositol Phosphates / Q000378:metabolism; D007421:Intestine, Small / Q000201:enzymology*; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D051381:Rats
D007295:Inositol Phosphates; D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; C021822:myo-inositol-1 (or 4)-monophosphatase; D010832:6-Phytase