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The properties of the pyridoxal kinase of mouse brain were studied and the following results were obtained.<br>1. It was concluded that toxopyrimidine seemed to be phosphorylated by the same phosphokinase as pyridoxal based on the following reasons: the mutual competitive inhibition, the coincidence of the metal requirements, the denaturation effects of heat treatment on the enzyme and the behaviors of inhibitors for both substrates.<br>2. The substrate specificities of the pyridoxal-kinase were investigated and the following results were obtained: (a) The pyridoxal-kinase was able to act on both certain pyridine and pyrimidine derivatives (b) The 2-methyl of the pyrimidine ring was able to be substituted with C2H5 or SCH3 group for CH3 group (c) The 4 position of the pyridine ring was able to be substituted with CH2OH, CH2NH2 or CH3 group for CHO group (d) The compounds without a hydroxymethyl group in the 5 position of the pyridine ring were not phosphorylated at all (such as pyrithioxine) or slightly phosphorylated in such a special case as 5-deoxypyridoxine
収録刊行物
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- THE JOURNAL OF VITAMINOLOGY
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THE JOURNAL OF VITAMINOLOGY 15 (2), 131-141, 1969
日本ビタミン学会
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詳細情報 詳細情報について
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- CRID
- 1390282681299900544
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- NII論文ID
- 130001749265
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- NII書誌ID
- AA00247734
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- COI
- 1:CAS:528:DyaF1MXksFKqt7w%3D
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- NDL書誌ID
- 8506207
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- ISSN
- 00225398
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- PubMed
- 5347447
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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
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可