Dehydrogenases of the Plasma Membrane

Crane, F.L.; Goldenberg, Hans; Morré, D. James; Löw, H.

doi:10.1007/978-1-4615-7945-8_6

Cited by 51 publications

(16 citation statements)

References 289 publications

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“…However, our H202-generating enzyme activity may not be identical with them, since xanthine oxidase is cyanide-sensitive and NADPH-cytochrome c reductase is localized on the baso-lateral membrane of the absorptive cells. An NADH-cytochrome c reductase activity is demonstrated in many tissues (2). This enzyme is sensitive to cyanide, thus, unlike our enzyme activity.…”

Section: Effects Of Several Inhibitorscontrasting

confidence: 51%

“…The reaction was most intense after a 10 min fixation (Table 1). This may be explained by the fact that extracellularly added substrates easily go through the fixed membrane and reach reaction sites for pyridine nucleotides, where are generally believed to be at the cytoplasmic side of the plasma membrane (2). Prolonged fixation caused much less precipitation, indicating probable denaturation of proteins which catalyze the CP precipitation.…”

Section: Effect Of Fixation With Glutaraldehydementioning

confidence: 99%

“…Crane et al (2) have emphasized the role of azide-and fluoride-sensitive NADH dehydrogenase (possibly NADH-cytocrome b5 reductase) for active transport of carnitine (vitamin BT) and other several substances. This enzyme is also insensitive to cyanide and inhibited by lack of oxygen.…”

Section: Effects Of Several Inhibitorsmentioning

confidence: 99%

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Electron cytochemical studies on an NAD(P)H-dependent H2O2-generating enzyme activity in the rat small intestine.

Ishikawa¹,

Hirai²,

Ogawa³

1981

Acta Histochem. Cytochem

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Section: Effects Of Several Inhibitorscontrasting

confidence: 51%

Section: Effect Of Fixation With Glutaraldehydementioning

confidence: 99%

See 1 more Smart Citation

Electron cytochemical studies on an NAD(P)H-dependent H2O2-generating enzyme activity in the rat small intestine.

Ishikawa¹,

Hirai²,

Ogawa³

1981

Acta Histochem. Cytochem

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“…The NADH dehydrogenase system responsible for reduction of ferricyanide or dichloroindophenol showed large activities as compared to NADPH-linked dehydrogenase, with the exception of dehydrogenase catalyzing glyoxylate reduction. The ratio of NADH-ferricyanide reductase: NADH cytochrome c reductase activity was 4.0, according to the data in table 2 (a mean value of the 3 preparations), while in chromaffin granules this ratio was 0.4 [17], indicating that this is plasma membrane dehydrogenase. Cytochrome b-561 in chromaffin granules faces cytoplasmic exterior and is ascorbate reducible in situ.…”

Section: ~Perime~almentioning

confidence: 73%

Interaction of antimycin with cytochrome b‐561

1983

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Cytochrome b-561 in chromaffin granules interacts with antimycin and its a-peak shifts 1 nm towards red. When chromaffin granules were treated with Triton X-100 antimycin no effect was observed. Cytochrome b-561 is located in the plasma membrane isolated from the chromaffin cells. The plasma membrane b-561does not seem to interact with antimycin. A number of NADH or NADPH (acceptor) oxidoreductase activity has been observed in isolated plasma membrane providing clues to the origin of plasma membrane dehydrogenase. The possible role of cytochrome b-561 in secretory granules other than its accredited energy conserving electron transport property is projected.

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“…The surface of plant cells (cell wall/plasmalemma interface) is an important site of redox reactions [2,3] and some of these are catalyzed by NADH oxidase/peroxidase that can lead to the generation of superoxide anion and hydrogen perox ide [4]. The latter appear to be involved in senescence, wounding and response of plant to biotic and abiotic • Corresponding author.…”

Section: Introductionmentioning

confidence: 99%