منابع مشابه
Pyridine coenzymes of subcellular tissue fractions.
The levels of pyridine nucleotides in tissues have been the subject of a large number of reports. Much interest has been focused on the ratios of oxidized to reduced coenzymes in different pathological conditions (1). Recently, Glock and McLean (2) have reported the important observation that reduced TPN is present in whole rat liver in comparatively large amounts, whereas the concentration of ...
متن کاملBinding of pyridine coenzymes to the beta-subunit of the voltage sensitive potassium channels.
The beta-subunit of the voltage-sensitive K(+) channels shares 15-30% amino acid identity with the sequences of aldo-keto reductases (AKR) genes. However, the AKR properties of the protein remain unknown. To begin to understand its oxidoreductase properties, we examine the pyridine coenzyme binding activity of the protein in vitro. The cDNA of K(v)beta2.1 from rat brain was subcloned into a pro...
متن کاملBinding of pyridine nucleotide coenzymes to the beta-subunit of the voltage-sensitive K+ channel.
The beta-subunit of the voltage-sensitive K(+) (K(v)) channels belongs to the aldo-keto reductase superfamily, and the crystal structure of K(v)beta2 shows NADP bound in its active site. Here we report that K(v)beta2 displays a high affinity for NADPH (K(d) = 0.1 micrometer) and NADP(+) (K(d) = 0.3 micrometer), as determined by fluorometric titrations of the recombinant protein. The K(v)beta2 a...
متن کاملDifferential regulation of voltage-gated K+ channels by oxidized and reduced pyridine nucleotide coenzymes.
The activity of the voltage-sensitive K+ (Kv) channels varies as a function of the intracellular redox state and metabolism, and several Kv channels act as oxygen sensors. However, the mechanisms underlying the metabolic and redox regulation of these channels remain unclear. In this study we investigated the regulation of Kv channels by pyridine nucleotides. Heterologous expression of Kvalpha1....
متن کاملCovalently bound Flavin Coenzymes.
Following elucidation of the structures of the flavin components of succinate dehydrogenase (SD) as N (3)-histidyl-8a-FAD and of monoamine oxidase (MAO) as cysteinyl-8a-FAD and determination of the peptide sequences around the flavin sites of these enzymes, attention has been focused on the covalently bound FAD of Chromatium cytochrome c-552. As documented in preliminary communications, the FAD...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1961
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)64328-5