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. 1984 Sep;76(1):40–44. doi: 10.1104/pp.76.1.40

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

Subhash C Gumber 1, Mary W Loewus 1, Frank A Loewus 1
PMCID: PMC1064223  PMID: 16663819

Abstract

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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Selected References

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