Oxidation-reduction potentials of the triphosphopyridine nucleotide system.
نویسندگان
چکیده
Triphosphopyridine nucleotide serves as the primary hydrogen or electron acceptor in a variety of biological oxidations. Some dehydrogenases like glucose g-phosphate dehydrogenase (1) and isocitric acid dehydrogenase (2) have an absolute requirement for TPN. Other systems such as liver glutamic acid dehydrogenase (3, 4) can utilize either TPN or DPN about equally well. In addition, a large number of dehydrogenases are known which have an absolute requirement for DPN. Although DPN and TPN have many similarities in structure and function, the available evidence indicates that the two coenzymes do not interact readily. Transfer of hydrogen between the nucleotides must be enzymatically catalyzed in both bacterial (5) and mammalian systems (6, 7). Glock and McLean (8) have shown that the concentration of DPN is greater than that of TPN in most tissues. Furthermore, most of the DPN is present in the oxidized form, but most of the TPN is present in the reduced form. A specific requirement for TPNH has been shown by Langdon (9) for the reductive synthesis of fatty acids in mammalian liver. The purpose of the present study was to determine the oxidation-reduction potentials of the TPN system and to compare them with the values determined for the DPN system.
منابع مشابه
Oxidation-Reduction Potentials of the Triphosphopyridine Nucleotide Svstem*
Triphosphopyridine nucleotide serves as the primary hydrogen or electron acceptor in a variety of biological oxidations. Some dehydrogenases like glucose g-phosphate dehydrogenase (1) and isocitric acid dehydrogenase (2) have an absolute requirement for TPN. Other systems such as liver glutamic acid dehydrogenase (3, 4) can utilize either TPN or DPN about equally well. In addition, a large numb...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 38 5 شماره
صفحات -
تاریخ انتشار 1952