Equilibrium Dialysis Measurements of the Ca^<2+>-Binding Properties of Recombinant Radish Vacuolar Ca^<2+>-Binding Protein Expressed in Escherichia coli(Biochemistry & Molecular Biology)

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概要

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• Vacuoles of radish (Raphanus sativus) contained a Ca^<2+>-binding protein (RVCaB) of 43 kDa. We investigated the Ca^<2+>-binding properties of the protein. RVCaB was expressed in Escherichia coli and was purified from an extract by ion-exchange chromatography, nitrocellulose membrane filtration, and gel-filtration column chromatography. Ca^<2+>-binding properties of the recombinant protein were examined by equilibrium dialysis with ^<45>Ca^<2+> and small dialysis buttons. The protein was estimated to bind 19Ca^<2+> ions per molecule with a K_d for Ca^<2+> of 3.4 mM. Ca^<2+> was bound to the protein even in the presence of high concentrations of Mg^<2+> or K^+. The results suggested that the protein bound Ca^<2+> with high ion selectivity, high capacity, and low affinity.

• 社団法人日本農芸化学会の論文
• 2002-11-23

著者

• Maeshima Masayoshi

  Graduate School Of Bioagricultural Sciences Nagoya University

• Maeshima M

  Nagoya Univ. Graduate School Of Bioagricultural Sci. Nagoya Jpn

• Yuasa Koji

  Graduate School Of Bioagricultural Sciences Nagoya University:(present Address)laboratory For Struct

• Yasuda Koji

  Graduate School of Bioagricultural Sciences, Nagoya University:(Present address)Laboratory for Structural Construction, RIKEN Plant Science Center

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