scholarly journals Neuromodulatory effect of solvent fractions of Africa eggplant (Solanium dadyphyllum) against KCN-induced mitochondria damage, viz. NADH-succinate dehydrogenase, NADH- cytochrome c reductase, and succinate-cytochrome c reductase

2018 ◽  
Vol 4 (1) ◽  
Author(s):  
Efe Obade ◽  
Omotayo B. Ilesanmi ◽  
Olamide Crown ◽  
Afolabi C. Akinmoladun ◽  
Tolulope M. Olaleye ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Succinate Dehydrogenase ◽  
Cytochrome C Reductase ◽  
Effect Of Solvent ◽  
Succinate Cytochrome C Reductase ◽  
Nadh Cytochrome

scholarly journals Properties of a cytochrome c-enriched light particulate fraction isolated from the photosynthetic bacterium Rhodopseudomonas spheroides

1978 ◽  
Vol 174 (1) ◽  
pp. 267-275 ◽  
Author(s):  
J Barrett ◽  
C N Hunter ◽  
O T G Jones
Keyword(s):  
Cytochrome C ◽  
Sodium Dodecyl ◽  
Photosynthetic Bacterium ◽  
Particulate Fraction ◽  
Cytochrome C Reductase ◽  
Cytochrome C2 ◽  
Succinate Cytochrome C Reductase ◽  
Bulk Membrane ◽  
Nadh Cytochrome ◽  
Rhodopseudomonas Spheroides

Differential centrifugation of suspensions of French-press-disrupted Rhodopseudomonas spheroides yielded a light particulate fraction that was different in many properties from the bulk membrane fraction. It was enriched in cytochrome c and had a low cytochrome b content. When prepared from photosynthetically grown cells this fraction had a very low specific bacteriochlorophyll content. The cytochrome c of the light particles differed in absorption maxima at 77K from cytochrome c2 attached to membranes; there was pronounced splitting of the alpha-band, as is found in cytochrome c2 free in solution. Potentiometric titration at A552–A540 showed the presence of two components that fitted an n = 1 titration; one component had a midpoint redox potential of +345mV, like cytochrome c2 in solution, and the second had E0′ at pH 7.0 of +110 mV, and they were present in a ratio of approx. 2:3. Difference spectroscopy at 77K showed that the spectra of the two components were very similar. More of a CO-binding component was present in particles from photosynthetically grown cells. Light membranes purified by centrifugation on gradients of 5–60% (w/w) sucrose retained the two c cytochromes; they contained no detectable succinate-cytochrome c reductase or bacteriochlorophyll and very little ubiquinone, but they contained NADH-cytochrome c reductase and some phosphate. Electrophoresis on sodium dodecyl sulphate/polyacrylamide gels showed that the light membranes of aerobically and photosynthetically grown cells were very similar and differed greatly from other membrane fractions of R. spheroides.

VALUE OF CONTROL THEORY IN THE STUDY OF CELLULAR METABOLISM — BIOMEDICAL IMPLICATIONS

1995 ◽  
Vol 03 (01) ◽  
pp. 165-175 ◽  
Author(s):  
MONIQUE MALGAT ◽  
THIERRY LETELLIER ◽  
SOPHIE L. JOUAVILLE ◽  
JEAN-PIERRE MAZAT
Keyword(s):  
Cytochrome C ◽  
Control Theory ◽  
Metabolic Networks ◽  
Threshold Effect ◽  
Cytochrome C Reductase ◽  
Succinate Cytochrome C Reductase ◽  
Nadh Cytochrome ◽  
Metabolic Control Theory ◽  
Control Coefficients

We use some examples to show that Metabolic Control Theory (MTC) not only allows the determination of the controlling steps of a metabolic network with the so-called control coefficients, but also leads to better understanding of the functioning of metabolic networks. The examples are taken partly from our own work on mitochondrial myopathies, partly from the literature: — the threshold effect observed in mitochondria diseases; — the problem of the diagnosis of complex I, II or III defects by measuring the NADH-cytochrome-c-reductase or the succinate-cytochrome-c-reductase activities with illustration by some cases. The possibility of a sum of control coefficients greater than one is also considered.

scholarly journals GTP- and inositol 1,4,5-trisphosphate-induced release of 45Ca2+ from a membrane store co-localized with pancreatic-islet-cell plasma membrane

1988 ◽  
Vol 253 (1) ◽  
pp. 67-72 ◽  
Author(s):  
M E Dunlop ◽  
R G Larkins
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Cytochrome C ◽  
Succinate Dehydrogenase ◽  
Close Association ◽  
Receptor Activation ◽  
Pancreatic Islet Cell ◽  
Cytochrome C Reductase ◽  
Inositol 1,4,5 Trisphosphate ◽  
Nadh Cytochrome

Inositol 1,4,5-trisphosphate [Ins(1,4,5)P3], arising from hydrolysis of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2], is proposed as the link between membrane-receptor activation and mobilization of Ca2+ from intracellular sites in hormone-secreting cells. The location of Ins(1,4,5)P3-sensitive membranes was investigated in cultured neonatal beta-cells. Membranes were obtained after lysis of cells attached to positively charged Sephadex. After lysis the presence of the enzyme markers 5′-nucleotidase, glucose-6-phosphatase, NADH-cytochrome c reductase, UDP-galactosyltransferase and succinate dehydrogenase indicated the mixed nature of the preparation. After sonication, however, UDP-galactosyltransferase and succinate dehydrogenase activities were undetectable, but 4.8% of total cellular glucose-6-phosphatase and 3.4% of total cellular NADH-cytochrome c reductase remained with 5′-nucleotidase in the preparation, indicating endoplasmic-reticulum association. ATP-dependent 45Ca2+ accumulation was shown in this preparation (410 +/- 24 pmol/mg of protein at 150 nM free Ca2+) and was inhibited by vanadate (100 microM). Ca2+ release was effected by Ins(1,4,5)P3, with half-maximal release at 0.5 +/- 0.14 microM-Ins(1,4,5)P3, t1/2 11.2 +/- 1.1 s. GTP- and guanosine 5′-[beta gamma-imido]triphosphate (p[NH]ppG)-promoted release of 45Ca2+ was demonstrated in this preparation, but the kinetics of release (half-maximal Ca2+ release at 5.4 +/- 0.7 microM, with t1/2 77.3 +/- 6.9 s, and at 51.1 +/- 4.2 microM, with t1/2 19.0 +/- 2.2 s, for GTP and p[NH]ppG respectively), and the ability of neomycin sulphate to block p[NH]ppG-induced release only, are indicative of separate release mechanisms after treatment with these agents. A close association between plasma membrane and elements of the endoplasmic reticulum is indicated in this model, providing a possible mechanism for local alterations in free Ca2+ in the sub-plasma-membrane region.

Endoplasmic reticulum membrane isolated from small-intestinal epithelial cells: enzyme and protein components

1981 ◽  
Vol 52 (1) ◽  
pp. 215-222
Author(s):  
M. Fujita ◽  
H. Ohta ◽  
T. Uezato
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Cytochrome C ◽  
Endoplasmic Reticulum Membrane ◽  
Dependent Manner ◽  
Cytochrome C Reductase ◽  
Basolateral Membranes ◽  
Nadh Cytochrome ◽  
Protein Components ◽  
A Minor

Endoplasmic reticulum membrane-rich fraction was obtained by subfractionation of the light microsomes from mouse jejunal mucosal epithelial cells. It was marked by high glucose-6-phosphatase, NADPH-cytochrome c reductase, and NADH-cytochrome c reductase activities and low Na+,K+-ATPase activity. The enrichment of Na+,K+-ATPase was 180-fold higher in the basolateral membranes than in the endoplasmic reticulum membrane-rich fraction relative to glucose-6-phosphatase. The protein peak that was phosphorylated in a Na-dependent manner was prominent in the basolateral membranes while it was a minor peak in the endoplasmic reticulum membrane-rich fraction. Under the electron microscope the fraction was seen to be composed of homogeneous small vesicles with thin smooth membranes.

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