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. 1984 Mar;74(3):510-5.
doi: 10.1104/pp.74.3.510.

Invertases of Lilium Pollen : Characterization and Activity during In Vitro Germination

M B Singh  1 , R B Knox
Affiliations

Invertases of Lilium Pollen : Characterization and Activity during In Vitro Germination

M B Singh et al. Plant Physiol. 1984 Mar.

Abstract

Two different forms of invertase are found in pollen of lily (Lilium auratum). One form is cytoplasmic (Invertase 1) and the other is bound to the pollen wall (Invertase 2). Invertase 1 has been partially purified and is a glycoprotein (apparent molecular weight, 450 kilodaltons) with a K(m) of 0.65 millimolar for sucrose. The two invertases differ in pH optimum and thermal stability. Invertases of lily pollen are beta-fructofuranosidases which can hydrolyze sucrose but not melizitose. The mature pollen grains have enzyme activity in both cytoplasmic and wall fractions, and no increase in the activity of either occurs during germination. The wall-bound enzyme could not be released by treatments with detergents or high salt concentrations.

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