Multiple Forms and Some Properties of Alkaline Phosphatase Produced by Aspergillus oryzae on Solid Medium

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概要

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• Three forms of alkaline phosphatase (Al-PMase) (EC. 3.1.3.1)were partially purified from Aspergillus oryzae grown on a bread medium which was in a phosphate-restricted condition. The purified enzymes were named Al-PMase I, II, and III, with pH optima at about pH 8, 99.5, and 10, respectively. Al-PMase II seems to be a major component in the Al-PMases of this fungus. The enzymes were satisfactorily stable at pH 710 at 30°C. Al-PMase I, II, and III were subjected to competitive inhibition with phosphate and commonly inhibited with Hg2+ and Mn2+. Al-PMase I and II were inhibited completely with EDTA, but Al-PMase III was insensitive to EDTA. Al-PMase II and III seemed to be a non-specific alkaline phosphatase. Al-PMase I showed less affinity to 5-nucleic acids than 2(3)-nucleic acids, and did not hydrolyze α-naphthyl phosphate, α-glycerophosphate, O-phosphoethanolamine, and phosphorylcholine.

著者

• Sakurai Yonekichi

  Department Of Agricultural Chemistry Faculty Of Agriculture Iwate University

• SHIOTA Hideo

  Department of Pharmacology, Graduate School of Biomedical Sciences, Nagasaki University

• TODA Katsuyoshi

  Department of Agricultural Chemistry, Faculty of Agriculture, Iwate University

関連論文

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• Multiple Forms and Some Properties of Alkaline Phosphatase Produced by Aspergillus oryzae on Solid Medium
• Growth and Respiratory Activity of Aspergillus oryzae Grown on Solid State Medium

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