[52] Preparations and properties of soluble NADH dehydrogenases from cardiac muscle

King, Tsoo E.; Howard, Robert

doi:10.1016/0076-6879(67)10055-4

Cited by 266 publications

(104 citation statements)

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“…Complex-I activity was measured spectrophotometrically by the method reported by King and Howard (1967). The method involves catalytic oxidation of NADH to NAD + with subsequent reduction of cytochrome c. The glycyl glycine (0.2 M) was prepared by dissolving 335 mg in 10 ml of phosphate buffer saline of pH 8.5.…”

Section: Complex-i (Nadh Dehydrogenase Activity)mentioning

confidence: 99%

Ameliorative effect of naringin against doxorubicin-induced acute cardiac toxicity in rats

Kwatra

Kumar

Jangra

et al. 2015

Pharmaceutical Biology

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Context: Doxorubicin (Dox) is one of the most active chemotherapeutic agents used to treat various types of cancers. Its clinical utility is compromised due to fatal cardiac toxicity characterized by an irreversible cardiomyopathy. Objective: This study evaluates the cardioprotective potential of naringin (NR) against Dox-induced acute cardiac toxicity in rats. Materials and methods: Male Wistar rats were randomly divided into five groups. NR (50 and 100 mg/kg) was administered intraperitoneally (i.p.) daily from 0 to 14 d. Doxorubicin (15 mg/kg, i.p.) was given as a single dose on the 10th day. On the 14th day, all animals were sacrificed and oxidative stress parameters that include malondialdehyde (MDA), glutathione (GSH) level, superoxide dismutase (SOD), catalase (CAT) activities, and all mitochondrial complexes (I-IV) activities were evaluated along with histopathological studies of the heart. Results: Doxorubicin-induced cardiotoxicity was confirmed by increased (p50.05) MDA, decreased (p50.05) GSH levels, SOD, and CAT activities, mitochondrial complexes (I-IV) activities in the heart tissue. NR (100 mg/kg) showed cardioprotection as evident from significant decreased MDA (p50.001) level, raised (p50.001) GSH level, SOD and CAT activities and increased mitochondrial complexes I (p50.01), II (p50.001), III (p50.001), and IV (p50.05) activities. Further, Dox-induced cardiotoxicity was confirmed by histopathological studies. These obtained results indicated the protective role of NR against Dox-induced cardiac toxicity in rats. Conclusion: NR can be used in combination with Dox due to its high cardioprotective effect against Dox-induced cardiomyopathy.

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Section: Complex-i (Nadh Dehydrogenase Activity)mentioning

confidence: 99%

Ameliorative effect of naringin against doxorubicin-induced acute cardiac toxicity in rats

Kwatra

Kumar

Jangra

et al. 2015

Pharmaceutical Biology

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“…The oxidation of NADH by homogenates was assayed in an Aminco-Bowman spectrophotofluorometer with potassium ferricyanide as an artificial electron acceptor (16 varied between 2.5 and 25 AM. Reaction mixture pH varied between 7.9 and 8.8.…”

mentioning

confidence: 99%

Mitrochondrial NADH dehydrogenase in cystic fibrosis.

Shapiro¹,

Feigal²,

Lam³

1979

Proc. Natl. Acad. Sci. U.S.A.

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We have shown that skin fibroblasts from patients with cystic fibrosis (CF) and from carriers for CF [heterozygotes (HZ)] consume more 02 than do their controls. When the mitochondrial electron transport inhibitor rotenone was added to the cells, the relative inhibition of 02 consumption was CF > HZ > controls (P < 0.005 in both comparisons). Because rotenone specifically inhibits NADH dehydrogenase, [NADH:(acceptor) oxidoreductase, EC 1.6.99.31, which is the enzyme of energy-conserving site 1 of the mitochondrial electron transport system, activity and kinetics of this enzyme system were studied in fibroblast homogenates. NADH dehydrogenase activity was equal in cells from the three genotypes. At pH 8.0, affinity of the enzyme for its substrate was CF < HZ = controls; at pH 8.6, affinity was CF> HZ = controls (P < 0.005 for the differences). pH optima for the genotypes were without exception 8.6 (CF), 8.3 (HZ), and 8.0 (control). HZ and control lines were distinguished unequivocally in a blind test on the basis of differences in pH optima. Purified mitochondrial preparations revealed pH optima identical to those found in whole cell homogenates. These data suggest that the mutant gene responsible for CF is expressed in the complex mitochondrial NADH dehydrogenase system.

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“…The Lactate dehydrogenase enzyme activity was estimated by the method of King [35]. The reaction mixture contained 0.5 ml of buffered substrate made in 0.1 M glycine buffer (pH 7.9) and 0.1 ml of tissue homogenate.…”

Section: Lactate Dehydrogenase Enzyme Activitymentioning

confidence: 99%

“…SDH was measured spectrophotometrically according to King [35]. The method involves oxidation of succinate by an artificial electron acceptor, potassium ferricyanide.…”

Section: Succinate Dehydrogenase (Sdh) Activity (Complex-ii)mentioning

confidence: 99%