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Further Studies on myo-Inositol-1-phosphatase from the Pollen of Lilium longiflorum Thunb ¹

Program in Biochemistry/Biophysics and the Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340

myo-Inositol-1-phosphatase has been purified to homogeneity from Lilium longiflorum pollen using an alternative procedure which includes pH change and phenyl Sepharose column chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis shows that the enzyme is a dimer (subunit molecular weight, 29,000 daltons). The enzyme is stable at low pH values and is inactivated only below pH 3.0. In addition to 1L-and 1D-myo-inositol-1-phosphate, it shows high specificity for 1L-chiro-inositol-3-phosphate. As observed earlier with other primary phosphate esters, D-glucitol-6-phosphate and D-mannitol-6-phosphate are hydrolyzed very slowly. No activity is observed with inorganic pyrophosphate or myo-inositol pentaphosphate as substrate. The enzyme is inhibited by fluoride, sulfate, molybdate, and thiol-directed reagents. Partial protection against N-ethylmaleimide inhibition by substrate and Mg²⁺ together suggests sulfhydryl involvement at the active site.

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