Inhibition of Acid Phosphatase Isoforms Purified from Mature Soybean (Glyczne MAX) Seeds |
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Authors: | Carmen Verissima Ferreira Eulazio Mikio Taga Hiroshi Aoyama |
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Affiliation: | 1. Departamento de Bioquimica, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970, Campinas, S?o Paulo, Brasilaoyama@unicamp.br;3. Departamento de Ciěncias Biológicas, Faculdade de Odontologia de Bauru, Universidade de S?o Paulo, 17043-101, Bauru, S?o Paulo, Brasil;4. Departamento de Bioquimica, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970, Campinas, S?o Paulo, Brasil |
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Abstract: | The four soybean seed acid phosphatase isoforms AP1, AP2, AP3A and AP3B were competitively inhibited by phosphate, vanadate, fluoride and molybdate, using p-nitrophenylphos-phate as substrate. The four isoforms were not significantly affected by compounds that can interact with SH residues or by pyridoxal phosphate. These results indicated that cysteine and lysine residues are not present in the active site of the four soybean seed acid phosphatase isoforms. The inhibition constant values for phosphate, vanadate, fluoride and molybdate at pH 5.0 were respectively: API (250, 12.8, 1.7, 0.05 μM), AP2 (800,10, 500, 0.025 μM), AP3A (250, 24.2,250, 0.032 μM), AP3B (2400, 36.9,750, 0.05 μM). |
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Keywords: | Acid phosphatase Soybean seed Inhibitors |
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