Abstract
Studies on the subcellular localization and selected properties of consitutive phosphohydrolases in pollen from Lilium longiflorum Thunb. (pH 5 phytase, pH 8 phytase, myo-inositol monophosphatase) are described. In anthers, all three enzymes increased in activity during pollen maturation along with levels of phytic acid. These enzymes were localized in mature pollen by the use of lead capture cytochemistry and shown to be associated with the membrane of the organelle previously identified as the storage site of phytic acid in the form of its insoluble salt, phytin. Recovery of the phytase with optimal activity at pH 8 was most complete when detergent or phospholipase C was included in the extracting medium, suggesting that its association with the organelle membrane is more integral than that of the other enzymes. The pH 8 phytase exhibited differences from a pH 5 phytase which has not been previously reported. They include higher substrate specificity for phytate, terminal hydrolysis to myo-inositol trisphosphate (stereochemistry undetermined), and lack of inhibition of fluoride. Our results suggest a subcellular organization of phytic acid metabolism in lily pollen with the pH 8 phytase as an important component.
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