Inhibitors of the transhydrogenase activity of spinach ferredoxin-Nicotinamide adenine dinucleotide phosphate reductase.

نویسندگان

  • W W Fredricks
  • J M Kohlmann
چکیده

Boiled spinach extracts reversibly inhibit the transhydrogenase activity of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase. The inhibition is competitive with respect to NAD but noncompetitive with respect to NADPH. The inhibitor is most effective at a pH of about 8.0. The inhibitor is characterized as an organic acid but does not appear to be a carbohydrate or phosphoric acid derivative or phosphodoxin. A number of compounds with inhibitory activity have been found. These compounds share the common chemical feature of having a vie-carbonyl gouping and include a number of cr-keto acids.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 244 4  شماره 

صفحات  -

تاریخ انتشار 1969