Abstract
We previously reported the purification of an acid phosphatase (APase52) secreted from the mycelia ofPholiota nameko under phosphate-deficient conditions. In the present study, two other isozymes (APase47 and APase48) were found and their structures were compared with that of APase52. Thirteen amino acid residues at theN-terminus of APase47 were completely identical with those of APase48 and had partial homology with those of APase52. The deglycosylation of proteins indicated that three APase isozymes differ in theN-linked oligosaccharide content. The protease-generated peptide maps of the APases differed from one another in the band pattern. These results suggest that the APases are the products of different genes.
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Yazaki, J., Joh, T., Tomida, Si. et al. Acid phosphatase isozymes secreted under phosphate-deficient conditions inPholiota nameko . Mycoscience 38, 347–350 (1997). https://doi.org/10.1007/BF02464095
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DOI: https://doi.org/10.1007/BF02464095