Purification and Some Properties of Acid β-Galactosidase from Pycnoporus cinnabarinus
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概要
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Acid β-galactosidase from Pycnoporus cinnabarinus was purified by precipitation with ammonium sulfate, column chromatographies on DEAE-Sephadex A-50,CM-Sephadex C-50 and Sephadex G-100,and isoelectric focusing. The purified enzyme appeared homogeneous on disc gel electrophoresis, and its molecular weight was about 110,000. The enzyme was most active at pH 2.4,and it was stable between pH 3 and 6 (for 2 hr at 37℃) and below 41℃ (for 15 min at pH 2.4). The K_m values of the enzyme were 0.95 mM for p-nitrophenyl β-D-galactoside and 33 mM for lactose.
- 1981-08-25
著者
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Hayashi Nobuo
Department Of Computer Science University Of Electro-communications
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Mitsutomi Masaru
Department Of Agricultural Chemistry Faculty Of Agriculture Saga University
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Ohtakara Akira
Department Of Agricultural Chemistry Faculty Of Agriculture Saga University
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Hayashi Nobuo
Department Of Agricultural Chemistry Faculty Of Agriculture Saga University
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