Singh M B, Knox R B
Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052, Australia.
Plant Physiol. 1984 Mar;74(3):510-5. doi: 10.1104/pp.74.3.510.
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.
在天香百合（Lilium auratum）的花粉中发现了两种不同形式的转化酶。一种形式是细胞质中的（转化酶1），另一种与花粉壁结合（转化酶2）。转化酶1已被部分纯化，是一种糖蛋白（表观分子量为450千道尔顿），对蔗糖的K(m)为0.65毫摩尔。这两种转化酶在最适pH值和热稳定性方面存在差异。天香百合花粉的转化酶是β-呋喃果糖苷酶，可水解蔗糖但不能水解松三糖。成熟花粉粒在细胞质和壁部分都具有酶活性，在萌发过程中两种酶的活性均未增加。用去污剂或高盐浓度处理无法释放与壁结合的酶。
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