Mode of binding of pyridoxal 5'-phosphate in rat liver ornithine aminotransferase.
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- SANADA Yukihiro
- Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicine, Tokushima University
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- SHIOTANI Taiichi
- Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicine, Tokushima University
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- KATUNUMA Nobuhiko
- Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicine, Tokushima University
Bibliographic Information
- Other Title
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- Mode of Binding of Pyridoxal 5′-Phosphate in Rat Liver Ornithine Aminotransferase
- Mode of Binding of Pyridoxal 5 Phosphat
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Abstract
1. Pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate were effective for the association of apo-form II of ornithine amino transferase [EC 2. 6. 1. 13]; whereas other B6 derivatives, such as pyridoxal, pyridoxamine, pyridoxine and pyridoxine 5'-phosphate, had no effect on form II of this apoenzyme.<br> 2. The pyridoxal 5'-phosphate contents of the native enzyme, and reconstituted forms I and II were determined by two different methods to be 1.5 moles, 2.5 moles and 3.3 moles of pyridoxal 5'-phosphate/mole of enzyme, respectively.
Journal
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- Journal of Nutritional Science and Vitaminology
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Journal of Nutritional Science and Vitaminology 24 (2), 77-82, 1978
Center for Academic Publications Japan
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Details 詳細情報について
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- CRID
- 1390282681303306752
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- NII Article ID
- 130001372207
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- NII Book ID
- AA00703822
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- ISSN
- 18817742
- 03014800
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- NDL BIB ID
- 1937220
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- PubMed
- 671110
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed