The behavior of cytoplasmic membranes in Phaseolus vulgaris cotyledons during germination

1974 ◽  
Vol 52 (3) ◽  
pp. 535-541 ◽  
Author(s):  
J. E. Thompson
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Molecular Complexes ◽  
Cytochrome C Reductase ◽  
Membrane Structure And Function ◽  
Cytoplasmic Membranes ◽  
Microsomal Membranes ◽  
Membrane Bound ◽  
Nadh Cytochrome ◽  
And Function

Information about the effects of germination on cytoplasmic membranes of cotyledons has been obtained by examining selected properties of smooth microsomes purified from cotyledon tissue at various stages of germination. The microsomal membranes contained rotenone-insensitive NADH – cytochrome c reductase (EC. 1.6.99.3) and NADPH – cytochrome c reductase (EC. 1.6.99.1). Measurements of these enzymes in smooth microsomal fractions isolated from various ages of cotyledon tissue revealed that their activities markedly decrease during the late stages of germination, coincident with onset of cotyledon senescence. This decrease is closely paralleled by a corresponding decline in total levels of the enzymes in the cotyledons during the same period, and has been interpreted as reflecting deterioration of cytoplasmic membrane structure and function concurrent with the progression of senescence. The membrane-bound cytochrome c reductase activity does not appear to be solubilized as a result of this deterioration. Furthermore, the protein:phospholipid ratios for the smooth microsomal preparations remain essentially unchanged during germination. This suggests that the macro-molecular complexes of membranes disaggregate more or less spontaneously during senescence and that in the process, the cytochrome c reductases are inactivated.

scholarly journals Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cell.

1979 ◽  
Vol 83 (1) ◽  
pp. 231-239 ◽  
Author(s):  
S R Slaughter ◽  
D E Hultquist
Keyword(s):  
Endoplasmic Reticulum ◽  
Cytochrome C ◽  
Dimethyl Sulfoxide ◽  
Reductase Activity ◽  
Cytochrome B5 ◽  
Erythroid Cells ◽  
Friend Virus ◽  
Cytochrome C Reductase ◽  
Membrane Bound ◽  
Nadh Cytochrome

We have obtained and studied a 105,000-g pellet from T-3-Cl-2 cells, a cloned line of Friend virus-induced erythroleukemia cells. By difference spectrophotometry, the pellet was shown to contain cytochrome b5 and cytochrome P-450, hemeproteins that have been shown to participate in electron-transport reactions of endoplasmic reticulum and other membranous fractions of various tissues. The pellet also possesses NADH-cytochrome c reductase activity which is inhibited by anti-cytochrome b5 gamma-globulin, indicating the presence of cytochrome b5 reductase. This is the first demonstration of membrane-bound forms of these redox proteins in erythroid cells. Dimethyl sulfoxide-treated T-3-Cl-2 cells were also shown to possess membrane-bound cytochrome b5 and NADH-cytochrome c reductase activity. We failed to detect soluble cytochrome b5 in the 105,000-g supernatant fraction from homogenates of untreated or dimethyl sulfoxide-treated T-3-Cl-2 cells. In contrast, erythrocytes obtained from mouse blood were shown to possess soluble cytochrome b5 but no membrane-bound form of this protein. These findings are supportive of our hypothesis that soluble cytochrome b5 of erythrocytes is derived from endoplasmic reticulum or some other membrane structure of immature erythroid cells during cell maturation.

Brain Regional Analysis of NADH-Cytochrome C Reductase Activity in Alzheimerʼs Disease

1990 ◽  
Vol 49 (3) ◽  
pp. 206-214 ◽  
Author(s):  
GEORGE S. ZUBENKO ◽  
JOHN MOOSSY ◽  
DIANA CLAASSEN ◽  
A. Julio Martinez ◽  
GUTTI R. RAO
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Regional Analysis ◽  
Cytochrome C Reductase ◽  
Nadh Cytochrome

scholarly journals Structural and functional relationships of enzyme activities induced by nitrate in barley

1970 ◽  
Vol 119 (4) ◽  
pp. 715-725 ◽  
Author(s):  
John L. Wray ◽  
Philip Filner
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Bottom Layer ◽  
Sucrose Density Gradient ◽  
Enzyme Complex ◽  
Cytochrome C Reductase ◽  
Functional Relationships ◽  
Nadh Cytochrome

1. Nitrate induces the development of NADH-nitrate reductase (EC 1.6.6.1), FMNH2–nitrate reductase and NADH–cytochrome c reductase activities in barley shoots. 2. Sucrose-density-gradient analysis shows one band of NADH–nitrate reductase (8S), one band of FMNH2–nitrate reductase activity (8S) and three bands of NADH–cytochrome c reductase activity (bottom layer, 8S and 3.7S). Both 8S and 3.7S NADH–cytochrome c reductase activities are inducible by nitrate, but the induction of the 8S band is much more marked. 3. The 8S NADH–cytochrome c reductase band co-sediments with both NADH–nitrate reductase activity and FMNH2–nitrate reductase activity. Nitrite reductase activity (4.6S) did not coincide with the activity of either the 8S or the 3.7S NADH–cytochrome c reductase. 4. FMNH2–nitrate reductase activity is more stable (t½ 12.5min) than either NADH–nitrate reductase activity (t½ 0.5min) or total NADH–cytochrome c reductase activity (t½ 1.5min) at 45°C. 5. NADH–cytochrome c reductase and NADH–nitrate reductase activities are more sensitive to p-chloromercuribenzoate than is FMNH2–nitrate reductase activity. 6. Tungstate prevents the formation of NADH–nitrate reductase and FMNH2–nitrate reductase activities, but it causes superinduction of NADH–cytochrome c reductase activity. Molybdate overcomes the effects of tungstate. 7. The same three bands (bottom layer, 8S and 3.7S) of NADH–cytochrome c reductase activity are observed irrespective of whether induction is carried out in the presence or absence of tungstate, but only the activities in the 8S and 3.7S bands are increased. 8. The results support the idea that NADH–nitrate reductase, FMNH2–nitrate reductase and NADH–cytochrome c reductase are activities of the same enzyme complex, and that in the presence of tungstate the 8S enzyme complex is formed but is functional only with respect to NADH–cytochrome c reductase activity.

scholarly journals Inhibition and inactivation of NADH-cytochrome c reductase activity of bovine heart submitochondrial particles by the iron(III)-adriamycin complex

1990 ◽  
Vol 265 (3) ◽  
pp. 865-870 ◽  
Author(s):  
B B Hasinoff
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Inner Mitochondrial Membrane ◽  
Submitochondrial Particles ◽  
Cytochrome C Reductase ◽  
Fast Phase ◽  
Bovine Heart ◽  
Direct Binding ◽  
Nadh Cytochrome

The NADH-cytochrome c reductase activity of bovine heart submitochondrial particles was found to be slowly (half-time of 16 min) and progressively lost upon incubation with the Fe2(+)-adriamycin complex. In addition to this slow progressive inactivation seen on incubation, a reversible fast phase of inhibition was also seen. However, if EDTA was added to the incubation mixture within 15 s, the slow progressive loss in activity was largely preventable. Separate experiments indicated that EDTA removed about one-half of the iron from the Fe2(+)-adriamycin complex in about 40 s. These results indicated the requirement for iron for the inactivation process. Since the Vmax. for the fast phase of inhibition was decreased by the inhibitor, the inhibition pattern was similar to that seen for uncompetitive or mixed-type inhibition. The direct binding of both Fe3(+)-adriamycin and adriamycin to submitochondrial particles was also demonstrated, with the Fe3(+)-adriamycin complex binding 8 times more strongly than adriamycin. Thus binding of Fe3(+)-adriamycin to the enzyme or to the inner mitochondrial membrane with subsequent generation of oxy radicals in situ is a possible mechanism for the Fe3(+)-adriamycin-induced inactivation of respiratory enzyme activity.

NADH-cytochrome c reductase activity in cultured human lymphocytes

1976 ◽  
Vol 176 (1) ◽  
pp. 119-126 ◽  
Author(s):  
Russell A. Prough ◽  
Richard L. Imblum ◽  
Richard A. Kouri
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Human Lymphocytes ◽  
Cytochrome C Reductase ◽  
Nadh Cytochrome

Increased peak oxygen consumption of trained muscle requires increased electron flux capacity

1994 ◽  
Vol 77 (4) ◽  
pp. 1941-1952 ◽  
Author(s):  
D. M. Robinson ◽  
R. W. Ogilvie ◽  
P. C. Tullson ◽  
R. L. Terjung
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Reductase Activity ◽  
Tight Binding ◽  
Treadmill Running ◽  
Complex Iii ◽  
Peak Oxygen Consumption ◽  
Transport Capacity ◽  
Cytochrome C Reductase ◽  
Nadh Cytochrome

The importance of the training-induced increase in mitochondrial capacity in realizing the increase in maximal O2 consumption (VO2max) of trained muscle was evaluated using an isolated perfused rat hindlimb preparation at a high blood flow (approximately 80 ml.min-1.100 g-1) during tetanic contractions. Rats trained for 8-–12 wk by treadmill running exhibited an approximately 25% increase in muscle VO2max (5.62 +/- 0.31 to 7.06 +/- 0.64 mumol.min-1.g-1), an increase in mitochondrial enzyme activity (approximately 70% for cytochrome oxidase and approximately 55% for NADH cytochrome-c reductase), and an increase in tissue capillarity (14%) that is expected to increase the O2 exchange capacity of the tissue. Muscle VO2max of sedentary (n = 34) and trained (n = 30) animals was determined, and electron transport capacity was acutely managed with myxothiazol, a tight-binding inhibitor of complex III. Inhibition of complex III was similar among 1) the low- and high-oxidative fibers and 2) the superficial and deep mitochondrial populations within muscle. Inhibition of NADH cytochrome-c reductase activity resulted in reductions in muscle VO2max with similar dose responses (mean effective dose of approximately 0.2 microM) of myxothiazol added to the perfusion medium. The extraction of O2 by the contracting muscle decreased as VO2max declined. The increase in muscle VO2max observed in the muscle of trained animals was eliminated when its electron transport capacity was reduced to that observed in normal sedentary rat muscle. Thus, the exercise-induced adaptation of an increased muscle mitochondrial content appears to be essential for trained muscle to exhibit its increased O2 flux capacity. The results of the present experiment illustrate the importance of mitochondrial adaptations in muscle remodeled by exercise training.

Biosynthesis, utilization, and translocation of endogenous isomeric spin-labelled radioactive cytidinediphosphodiglycerides from isolated guinea pig liver microsomal to mitochondrial membranes

1979 ◽  
Vol 57 (7) ◽  
pp. 1019-1025 ◽  
Author(s):  
L. Stuhne-Sekalec ◽  
N. Z. Stanacev
Keyword(s):  
Cytochrome C ◽  
Guinea Pig ◽  
Reductase Activity ◽  
Mitochondrial Membranes ◽  
Pig Liver ◽  
Cytochrome C Reductase ◽  
Lipid Species ◽  
Microsomal Membranes ◽  
Guinea Pig Liver ◽  
Nadph Cytochrome C Reductase

When isolated guinea pig liver microsomal membranes were incubated with isomeric (5-, 12-, and 16-doxyl stearoyl) spin-labelled sn-3-[2-3H]phospfaatidic acid in the presence of CTP and Mg2+, formation of corresponding CDP-[2-3H]diglycerides (in an amount representing 16.5–17.4% of the labelled lipids), which were acceptable substrates in the microsomal biosynthesis of sn-3-[2-3H]phosphatidyl-myo-[U-l4C]inositols, took place. When microsomal membranes containing known amounts of labelled CDP-diglycerides were incubated with unlabeled mitochondrial membranes, reisolated mitochondria contained labelled lipids in an amount which could not be accounted for by the microsomal contamination of reisolated mitochondria, determined by the assay of NADPH – cytochrome c reductase activity, establishing therefore the translocation of labelled CDP-diglycerides (and other labelled lipids) from microsomal to mitochondrial membranes in an amount of ~50% of microsomal content. The rate of loss of paramagnetic lipid species in microsomal and in reisolated mitochondrial membranes was found to be quite different. When reisolated mitochondria containing trans-located isomeric spin-labelled CDP-[2-3H]diglycerides were further incubated with sn-3-[U-14C]glycerophosphate, the formation of labelled phosphatidylglycerophosphate and phosphatidylglycerol was detected. These findings established that the translocation of endogenously formed CDP-[2-3H]diglycerides occurred from isolated microsomal membranes to both outer and inner mitochondrial membranes.

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