INTRACELLULAR DISTRIBUTION OF DIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME c REDUCTASE AND CYTOCHROME c OXIDASE IN MAMMALIAN BRAIN

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Influence of metallic chelates on the diphosphopyridine nucleotide oxidase and diphosphopyridine nucleotide-cytochrome c reductase systems.

The need for additional study on the specific relation between metallic ions and metabolic function, especially in the case of the diphosphopyridine nucleotide oxidase system, has been expressed by Mahler (1) and others. This is particularly indicated in view of the fact that a number of the known components of this system contain iron. While it is broadly concluded that iron compounds facilita...

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The Influence of Metallic Chelates on the Diphosphopyridine Nucleotide Oxidase and Diphosphopyridine Nucleotide- Cytochrome c Reductase Systems*

The need for additional study on the specific relation between metallic ions and metabolic function, especially in the case of the diphosphopyridine nucleotide oxidase system, has been expressed by Mahler (1) and others. This is particularly indicated in view of the fact that a number of the known components of this system contain iron. While it is broadly concluded that iron compounds facilita...

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TRIPHOSPHOPYRIDINE NUCLEOTIDE - CYTOCHROME c REDUCTASE IN LIVER

In yeast the reduction of ferricytochrome c by reduced triphosphopyridine nucleotide (TPNH2) is catalyzed by a flavoprotein, cytochrome c reductase, which contains flavin mononucleotide (FMN, riboflavin phosphate) as the prosthetic group (1). In animal tissue the reduction of ferricytochrome c by TPNHz has not yet been reported, although the reaction with reduced diphosphopyridine nucleotide (D...

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The preparation and properties of a soluble diphosphopyridine nucleotide cytochrome c reductase.

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1952

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)55540-x