Purification and Some Properties of GTP Cyclohydrolase I from Spinach Leaves

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概要

• 論文の詳細を見る

• GTP cyclohydrolase I (EC 3.5.4.16) has been purified for the first time from a higher plant, spinach leaves. The purified preparation appeared to be homogeneous on polyacrylamide gel electrophoresis. The molecular weight of this enzyme was estimated at 135,000 by gel filtration and the subunit molecular weight was estimated at 35,000 by SDS-PAGE. The latter method also suggested that this enzyme was composed of four identical subunits. The enzyme was stable to heat treatment at 50℃ for 10 min, and the activity was maintained for at least six months when stored at -30℃. The enzyme had an optimum pH of around 8.0 in Tris buffer. The Hill coefficient of the enzyme was calculated to be 2.2. The pI of the enzyme was measured as 5.1 by chromatofocusing.

• 社団法人日本農芸化学会の論文
• 1997-07-23

著者

• Ohta Tomoko

  Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University

• MASADA Masahiro

  Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University

• SOHTA Yasuko

  Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University

• Masada Masahiro

  Department Of Biology Tokyo Metropolitan University

• Masada Masahiro

  Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University

• Sohta Yasuko

  Department Of Bioresources Chemistry Faculty Of Horticulture Chiba University

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