Phosphatases from pollen of Brassica campestris and Lilium regale |
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Authors: | Stanley Strother Mohanbir Singh Glenda Beresford R.Bruce Knox |
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Affiliation: | 1. Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria 3052 Australia |
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Abstract: | Soluble and wall-bound acid phosphatases isolated from rape seed pollen showed similar properties except for the pH optimum curve which was elevated for the cell wall enzyme. About 50 % of the phosphatase activity of washed pollen wall preparations could be solubilized with Triton X-100, compared with only ca 20% for the corresponding preparation from lily pollen. A comparison of the wall-bound acid phosphatase of rape seed and lily pollen showed a marked difference in specificity towards fructose-6-phosphate and glucose-6-phosphate. A Mg2+-dependent alkaline pyrophosphatase was obtained from rape seed pollen but this activity could not be detected in cell wall preparations. |
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Keywords: | Cruciferae rape seed Liliaceae pollen wall phosphatases. |
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