Characterization of High- and Low-Molecular Weight Zinc-Dependent Acid Phosphatases in Bovine Liver
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概要
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We have purified two forms of Zn^<2+>-dependent acid phosphatase (Zn^<2+>-APase) from bovine liver, both of which require Zn^<2+> to hydrolyze the substrate p-nitrophenyl phosphate in an acidic environment. The apparent molecular weights of these two forms of Zn^<2+>-APase were estimated to be about 100000 and 62000 by gel filtration, and about 44000 and 31000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, respectively. The low-molecular weight (LMW) Zn^<2+>-APase catalyzed the hydrolysis of myo-inositol-1-phosphate in the presence of 3 mM Mg^<2+> at physiological pH, but the high-molecular weight (HMW) enzyme did not. The LMW-Zn^<2+>-APase of bovine liver was recognized by polyclonal antibodies developed against the Zn^<2+>-APase of bovine brain, but the HMW-Zn^<2+>-APase was not.
- 公益社団法人日本薬学会の論文
- 1998-11-15
著者
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Shimohama S
Kyoto Univ. Kyoto Jpn
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Shimohama Shun
Department Of Neurology Faculty Of Medicine Kyoto University
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FUJIMOTO Sadaki
Department of Environmental Biochemistry, Kyoto Pharmaceutical University
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Fujimoto Sadaki
Department Of Environmental Biochemistry Kyoto Pharmaceutical University
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TANINO Hiroko
Department of Environmental Biochemistry, Kyoto Pharmaceutical University
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Tanino Hiroko
Department Of Environmental Biochemistry Kyoto Pharmaceutical University
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TSUDA Junji
Department of Environmental Biochemistry, Kyoto Pharmaceutical University
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KIMURA Takanobu
Department of Environmental Biochemistry, Kyoto Pharmaceutical University
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Tsuda J
Department Of Environmental Biochemistry Kyoto Pharmaceutical University
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Kimura Takanobu
Department Of Environmental Biochemistry Kyoto Pharmaceutical University
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FUJIMOTO Sadaki
Department of Biochemistry I Kyoto Pharmaceutical University:Department of III Kyoto Pharmaceutical University:Department of Pharmaceutical Chemistry II Kyoto Pharmaceutical University
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