Abstract
The glycosylphosphatidylinositol (GPI)-anchored phosphatase of S. oligorrhiza plants was a purple-colored metalloenzyme containing Fe and Mn atoms and its absorption spectrum had the maximum at 556 nm. Western blot experiment using anti-A. thaliana purple acid phosphatase (PAP) antibody showed that the S. oligorrhiza phosphatase cross-reacted with the antibody. These results suggest that the GPI-anchored phosphatase is a PAP. A 1.4 kbp cDNA clone was obtained from a S. oligorrhiza cDNA library by plaque hybridization using an A. thaliana PAP gene as a probe. The estimated amino acid sequence of this clone showed 82% and 80% similarity with the sequences of the A. thaliana and Phaseolus vulgaris PAPs, respectively.
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© 1997 Kluwer Academic Publishers
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Nakazato, H. et al. (1997). Characterization and cDNA cloning of the GPI-anchored phosphatase from Spirodela oligorrhiza . In: Ando, T., Fujita, K., Mae, T., Matsumoto, H., Mori, S., Sekiya, J. (eds) Plant Nutrition for Sustainable Food Production and Environment. Developments in Plant and Soil Sciences, vol 78. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0047-9_62
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DOI: https://doi.org/10.1007/978-94-009-0047-9_62
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