Purification and Some Properties of GTP Cyclohydrolase I from Spinach Leaves.
書誌事項
- タイトル別名
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- Purification and Some Properties of GTP
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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°C for 10 min, and the activity was maintained for at least six months when stored at -30°C. 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.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 61 (7), 1081-1085, 1997
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681453222656
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- NII論文ID
- 110002678651
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 4270694
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 使用不可