Results 131 to 140 of about 56,076 (155)
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Archives of Biochemistry and Biophysics, 1983
Inactive NADP-malate dehydrogenase (disulfide form) from chloroplasts of Zea mays is activated by reduced thioredoxin while the active enzyme (dithiol form) is inactivated by incubation with oxidized thioredoxin. This reductive activation of NADP-malate dehydrogenase is inhibited by over 95% in the presence of NADP and the Kd for this interaction of ...
Anthony R. Ashton, Marshall D. Hatch
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Inactive NADP-malate dehydrogenase (disulfide form) from chloroplasts of Zea mays is activated by reduced thioredoxin while the active enzyme (dithiol form) is inactivated by incubation with oxidized thioredoxin. This reductive activation of NADP-malate dehydrogenase is inhibited by over 95% in the presence of NADP and the Kd for this interaction of ...
Anthony R. Ashton, Marshall D. Hatch
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Crystal Structures of a Ferredoxin: NADP+ Reductase and of a Complex with NADP+
Biochemical Society Transactions, 1996Michel Frey+5 more
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Complex formation of ferredoxin-NADP reductase with ferredoxin and with NADP
Biochemical and Biophysical Research Communications, 1968Anthony San Pietro, Masateru Shin
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Archives of Biochemistry and Biophysics, 2003
The apparent equilibrium constant of the biochemical reaction, 2-propanol+NADP(ox) = acetone+NADP(red), was determined at I = 0.25 M over a wide range of pH (5.63 to 8.02) and temperature (5 to 40 degrees C). The reaction was catalyzed by an NADP-dependent alcohol dehydrogenase.
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The apparent equilibrium constant of the biochemical reaction, 2-propanol+NADP(ox) = acetone+NADP(red), was determined at I = 0.25 M over a wide range of pH (5.63 to 8.02) and temperature (5 to 40 degrees C). The reaction was catalyzed by an NADP-dependent alcohol dehydrogenase.
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Comparison of Thio-NADP⊕and Seleno-NADP⊕in NADP⊕-Dependent Oxidoreductases
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1970Helmut Coper+2 more
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