Abstract |
A NADH-ferricyanide reductase of the external surface of intact mouse ascites tumor cells grown in culture was shown. The oxidation/reduction reaction was due to enzymatic rather than inorganic iron catalysis as demonstrated by the kinetics and specificity of the reaction. Activities of three markers for cytoplasmic contents were lacking with the intact tumor cells. The dehydrogenase activity was inhibited by p-chloromercuribenzoate, bathophenanthroline sulfonate, and the anticancer drug adriamycin. Sodium azide and potassium cyanide inhibited partially. The response to inhibitors resembled that of isolated plasma membranes rather than that of mitochondria. Concurrent with these findings, neither superoxide dismutase nor rotenone affected the redox activity. The findings provide evidence for the operation of a plasma membrane redox system at the surface of intact, living cells.
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Authors | J M Cherry, W Mackellar, D J Morré, F L Crane, L B Jacobsen, V Schirrmacher |
Journal | Biochimica et biophysica acta
(Biochim Biophys Acta)
Vol. 634
Issue 1
Pg. 11-8
(Jan 14 1981)
ISSN: 0006-3002 [Print] Netherlands |
PMID | 7470494
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Azides
- Chloromercuribenzoates
- Ferricyanides
- Doxorubicin
- L-Lactate Dehydrogenase
- Succinate Dehydrogenase
- NADH, NADPH Oxidoreductases
- ferricyanide reductase
- NADPH Dehydrogenase
- NADH Dehydrogenase
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Topics |
- Animals
- Azides
(pharmacology)
- Cell Membrane
(metabolism)
- Chloromercuribenzoates
(pharmacology)
- Doxorubicin
(pharmacology)
- Ferricyanides
(metabolism)
- Kinetics
- L-Lactate Dehydrogenase
(metabolism)
- Leukemia L5178
(metabolism, physiopathology)
- Leukemia, Experimental
(metabolism)
- Mice
- NADH Dehydrogenase
(metabolism)
- NADH, NADPH Oxidoreductases
(metabolism)
- NADPH Dehydrogenase
(metabolism)
- Neoplasm Metastasis
- Oxidation-Reduction
- Succinate Dehydrogenase
(metabolism)
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