[122] TPNH cytochrome c reductase from yeast

Haas, Erwin

doi:10.1016/s0076-6879(55)02286-6

Cited by 9 publications

(3 citation statements)

References 4 publications

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“…0.1 ml). The reaction was initiated by the addition of the subcellular fraction and the reduction of cytochrome c was followed at 550nm (Haas, 1955). The activity of the enzyme was calculated by using ACmM (reduced minus oxidized) of 27.7 (Haas, 1955).…”

Section: Assay Of Cytochrome C-nadph Reductasementioning

confidence: 99%

The mechanism of C-20 hydroxylation of α-ecdysone in the desert locust, Schistocerca gregaria

Johnson¹,

Rees²

1977

Biochemical Journal

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1. The C-20 hydroxylation of alpha-ecdysone to produce beta-ecdysone was investigated in the desert locust, Schistocerca gregaria. 2. alpha-Ecdysone C-20 hydroxylase activity was located primarily in the fat-body and Malpighian tubules. The properties of the hydroxylation system from Malpighian tubules investigated further. 3. The enzyme system was mitochondrial, had a pH optimum of 6.5, an apparent Km of 12.5 micron and required O2 and NADPH. 4. The activity of the hydroxylation system showed developmental variation within the fifth instar, the maximum activity corresponding to the maximum tire of endogenous moulting hormone. The significance of these results is assessed in relation to the control of the endogenous titre of beta-ecdysone. 5. The mechanism of the hydroxylation system was investigated by using known inhibitors of hydroxylation reactions such as CO, metyrapone and cyanide. 6. The CO difference spectrum of the reduced mitochondrial preparation indicated the presence of cytochrome P-450 in the preparation. 7. It concluded that the alpha-ecdysone C-20 hydroxylase system is a cytochrome P-450-deendent mono-oxygenase.

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Section: Assay Of Cytochrome C-nadph Reductasementioning

confidence: 99%

The mechanism of C-20 hydroxylation of α-ecdysone in the desert locust, Schistocerca gregaria

Johnson¹,

Rees²

1977

Biochemical Journal

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“…; ferrocytochrome c red/ox, 19 at 55onm. (Haas, 1955); vitamin K,, Oxidative phosphorylation in Anabaena 57 0.258 at 245 nm. The latter value was kindly supplied by Dr P. J. Dunphy of this department.…”

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confidence: 99%

Electron Transport and Oxidative Phosphorylation in the Blue-green Alga Anabaena variabilis

Leach

Carr

1970

Journal of General Microbiology

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S U M M A R YThe respiratory electron transport system involved in NADPH (2.0 nmoles/ min./mg.) and NADH (1.0 nmoles/min./mg.) oxidation in the dark that was operative in extracts of light-grown Anabaena variabilis has been examined.NADPH oxidation was inhibited 50 % by cyanide (2 x I O -~ M), rotenone (IO-* M); antimycin A, amytal and azide were markedly less inhibitory. NADPH : ferrocytochrome c oxidoreductase, NADPH : rnenadione oxidoreductase, ferrocytochrome c : oxygen oxidoreductase and succinic dehydrogenase were detected. A phosphorylation (0.4 nmoles/min./mg.), associated with NADPH oxidation, was measured, NADPH could be replaced by NADP and isocitrate. This phosphorylation was absolutely dependent upon oxygen and was inhibited 25 yo by carbonyl cyanide p-trifluoromethoxyphenylhydrazone (5 p~) .

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“…The values of rotenone-sensitive NADH cytochrome c-reductase activity were calculated as differences between the respective activities in the absence and again in the presence of rotenone. When evaluating the increase in enzymatic activity for cytochronie c, the niillimolar extinction coefficient of 28.1 was used (Haas, 1955).…”

Section: Met Hodsmentioning

confidence: 99%

Enzymatic activities in mitochondria isolated from the rat brain during development

Mourek

Průžzková

Svobodové

et al. 1975

Developmental Psychobiology

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In an attempt to discern whether mitochondrial changes during ontogeny are due to increases in number of mitochondria or to increases in number plus changes in their organization, we investigated the enzymatic markers of the inner and outer membranes of mitochondria from cerebral cortex and subcortical material in young and adult rats. We conclude from the data gathered that significant changes do occur in mitochondrial organization, that gradual maturation occurs in the inner membrane during development, especially in the cerebral cortex and considerably less so in the subcortical structures. We found no such changes in the sturucture of the outer membrane during the periods of development examined.

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[122] TPNH cytochrome c reductase from yeast

Cited by 9 publications

References 4 publications

The mechanism of C-20 hydroxylation of α-ecdysone in the desert locust, Schistocerca gregaria

The mechanism of C-20 hydroxylation of α-ecdysone in the desert locust, Schistocerca gregaria

Electron Transport and Oxidative Phosphorylation in the Blue-green Alga Anabaena variabilis

Enzymatic activities in mitochondria isolated from the rat brain during development

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