Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Infusion of 1 mul arachis oil containing 1.5 mug bis-(1 -methylethyl)phosphorofluoridate (di-isopropylfluorophosphate: DFP) into the caudate--putamen nucleus and substantia nigra of rats produced a considerable reduction of histochemical staining for acetylcholinesterase (AChE) in these two brain regions 30--120 min after injection. Thereafter, regeneration of AChE occurred within the zone of DFP effect. These new stores of AChE were associated with discrete neuronal perikarya and their processes. Intracerebral DFP administration had little or no histochemically detectable effect on NADH-diaphorase. Thionin staining was similarly unaffected. The results with punctate intracerebral application of DFP were replicated by intramuscular injection of 1.5 mg/kg DFP. Although the significance of dopaminergic--cholinergic interactions in the neostriatum could not be elucidated on the basis of these histochemical data, the thesis was advanced that dopamine neurons in the pars compacta of the substantia nigra also contained AChE, possibly to inactivate acetylcholine released from cholinergic fibers afferent to this neural structure.
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PMID:Acetylcholinesterase-containing neurons in the neostriatum and substantia nigra revealed after punctate intracerebral injection of di-isopropylfluorophosphate. 123 57

Molecular oxygen or cytochrome c has been described as the electron acceptor of the reaction of old yellow enzyme with NADPH. In this study, menadione was found to be a sensitive electron acceptor of the reaction under aerobic as well as anaerobic conditions. The Km value of menadione for old yellow enzyme is as low as 2-3 x 10(-7) M in the presence or absence of superoxide dismutase. The rate enhancement of the cytochrome c reduction of old yellow enzyme with NADPH was about eight times in the presence of menadione. The rate increment was slightly higher under aerobic than anaerobic conditions. The rate enhancement by menadione enabled sensitive determination of the enzyme activity in the assay system, which contained NADPH, cytochrome c, menadione, and old yellow enzyme. In the reaction course, the semiquinone species of menadione was trapped by the reaction with t-butyl-alpha-phenylnitrone. The radical adduct was detected on EPR. The dyestuff, 2,6-dichlorophenolindophenol, was found to be reduced ineffectively even in the presence of menadione; moreover, it was inhibitory in the NADPH consumption reaction. Methylene blue or Lauth's violet, known to be capable of semiquinone formation, also behaved, like menadione, as a mediator of electron transport to cytochrome c. On the basis of the experimental results, the occurrence of the one electron transfer of the old yellow enzyme reaction was emphasized.
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PMID:Characterization of the electron acceptors of old yellow enzyme: mechanistic approach to the mode of one electron transfer from the enzyme to menadione or dyestuffs. 813 46