Microsomal DPNH cytochrome C reductase

Penn, N. W.; Mackler, Bruce

doi:10.1016/0006-3002(58)90383-4

Cited by 28 publications

(5 citation statements)

References 13 publications

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“…Three-phase partitioning (TPP) was originally developed in the 1950s to purify proteins using 1-butanol in the upper phase and (NH 4 ) 2 SO 4 and pH in the aqueous lower phase (20). Low speed centrifugation will induce an interphase with precipitated proteins above the aqueous phase because butanol bound to proteins increases their buoyancy (21).…”

mentioning

confidence: 99%

New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy

Peltier¹,

Ytterberg²,

Sun

et al. 2004

Journal of Biological Chemistry

249

195

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confidence: 99%

New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy

Peltier¹,

Ytterberg²,

Sun

et al. 2004

Journal of Biological Chemistry

249

195

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“…The isolated flavoprotein reacts with cytochrome bs, but not with cytochrome c (86,87). The PCMBsensitive NADH-NT reductase (19), like its NADPH counterpart, probably contains an additional component (X2) besides the flavoprotein, perhaps iron (88). In the newborn, the low NADH-cytochrome c reductase activity is clearly not caused by rate limitation at the level of the flavoprotein or cytochrome b~ (see Fig.…”

mentioning

confidence: 99%

Biogenesis of Endoplasmic Reticulum Membranes

Dallner

Siekevitz

Palade

1966

The Journal of Cell Biology

561

112

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Thc constitutivc enzymes of microsomal mcmbrancs wcrc invcstigatcd during a pcriod of rapid ER dcvclopmcnt (from 3 days bcforc to 8 days aftcr birth) in rat hcpatocytcs. Thc activitics studicd (clcctron transport cnzymcs and phosphatascs) appcar at different times and incrcasc at diffcrcnt ratcs. Thc incrcasc in the cnzymc activitics tcstcd was inhibited by Actinomycin D and puromycin. G-6-Pasc and NADPH-cytochromc c rcductasc activities appcarcd first in thc rough microsomcs, and subscqucntly in smooth microsomcs, cvcntually reaching a uniform conccntration as in adult livcr. The cvidcncc suggcsts that thc cnzymcs arc synthcsizcd in the rough part, then transfcrrcd to thc smooth part, of the ER. Changcs in thc fat supplcmcnt of the maternal diet brought about changcs in thc fatty acid composition of microsomal phospholipids but did not influcncc thc enzymic pattcrn of thc suckling. Microsomcs from 3-day-old and adult rats losc 95 % of PLP and 80 % of NADHcytochromc c rcductasc activity after acctonc-H20 (I0: l) extraction. Howcvcr, onc-half thc original activity could bc rcgaincd by adding back phospholipid miccllcs prcparcd from purificd phospholipid, or from lipid extracts of heart mitochondria, or of liver microsomcs of 8~ay or adult rats, thus demonstrating an activation of thc enzymc by nonspccific phospholipid. Thc rcsults suggest that during dcvclopmcnt the cnzymic pattcrn is not influcnccd by the fatty acid or phospholipid composition of ER mcmbranes.

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“…Although the DPNH-cytochrome c reductase activity has been purified nine times, it is still associated with particles. Several soluble DPNHcytochrome c reductases are known from mammalian tissues, such as the one from pig heart described by Mahler et al (1952) ; one from beef liver microsomes (Penn and Markler, 1958); and one solubilized from beef heart electron transport particle by DeBernhard (1957). The properties of this group of enzymes are in general similar, and resemble those of the Proteus preparation described here, although here the activity remains associated with particles.…”

Section: Discussionmentioning

confidence: 99%

Some Additional Properties of Proteus Particles

Feldman

O’Kane

1960

J Bacteriol

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The localization of oxidative enzymes in the particulate fraction of cells is well known for many species. Pyruvate oxidation in Proteus vulgaris has been shown to require two fractions (Moyed and O'Kane, 1952); one of these was later shown to be particulate and to contain all the cytochromes of the cell (Moyed and O'Kane, 1956). Originally separated by ammonium sulfate fractionation, this fraction can also be separated by high speed centrifugation. This report describes some additional properties of these particles, and the partial purification of one of the activities, reduced diphosphopyridine nucleotide (DPNH)-cytochrome c reductase. MATERIALS AND METHODS Respiration. Conventional manometric methods were used at 37 C. The reaction mixture was made up to 3.0 ml with distilled water, and the center well contained 0.2 ml of 20 per cent KOH. The concentrations of buffer, preparation, substrate, and inhibitors are designated in the individual experiments. An equilibration period of 10 min was allowed before the tipping of substrate or enzyme preparation. Activity was calculated from the oxygen uptake and was expressed as ,umoles of substrate oxidized per minute per mg protein. Reduction of cytochrome c. The increase in optical density of the reaction mixture was measured at a wave length of 550 m,u and at a slit width of 0.02 mm on the Beckman model DU spectrophotometer. Each 1 cm cuvette contained 3 ml of the reaction mixture, which was 0.02 M with respect to either tris(hydroxymethyl)aminomethane (Tris) or phosphate buffer at the designated pH. Each cuvette contained in addition, 0.08 Amole of cytochrome c (based on dry wt, assuming a mol wt of 13,000) and 200 /g of ' Supported in part by a grant from the National Science Foundation.

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Microsomal DPNH cytochrome C reductase

Cited by 28 publications

References 13 publications

New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy

New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy

Biogenesis of Endoplasmic Reticulum Membranes

Some Additional Properties of Proteus Particles

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