Purification and Properties of Extracellular Acid Phosphatase from Zizania latifolia-parasite, Ustilago esculenta
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概要
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An extracellular acid phosphatase from Ustilago esculenta was purified to homogeneity on the basis of polyacrylamide gel electrophoresis. It was a glycoprotein with an isoelectric point of 4.7. The molecular weight of the enzyme was estimated to be about 343, 000 by gel filtration on Sephadex G-200, whereas on SDS-polyacrylamide gel electrophoresis, the enzyme gave a single protein band with a molecular weight of 116, 000. This result suggests that the enzyme consists of three identical subunits. The enzyme showed an optimum activity at pH 4.5, retained 90% of its activity for 10 min at 55°C and had a Km value of 0.25 mM for p-nitrophenylphosphate. No definite substrate specificity of the enzyme was observed.
- 社団法人 日本農芸化学会の論文
著者
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Funaguma Tooru
Laboratory Of Biological Chemistry Faculty Of Agriculture Meijo University
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Hara Akira
Laboratory Of Biochemistry And Nutritional Chemistry:(present Address)faculty Of Agriculture Meijo U
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Hara Akira
Laboratory of Biological Chemistry, Faculty of Agriculture, Meijo University
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KAWAMURA Yoshikazu
Laboratory of Biological Chemistry, Faculty of Agriculture, Meijo University
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