Results 161 to 170 of about 590,505 (211)
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Cytochrome C-Mediated Apoptosis
Annual Review of Biochemistry, 2004▪ Abstract Apoptosis, or programmed cell death, is involved in development, elimination of damaged cells, and maintenance of cell homeostasis. Deregulation of apoptosis may cause diseases, such as cancers, immune diseases, and neurodegenerative disorders. Apoptosis is executed by a subfamily of cysteine proteases known as caspases. In mammalian cells,
Xuejun, Jiang, Xiaodong, Wang
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Multiple cytochromes b in Mycobacterium phlei
Biochemical and Biophysical Research Communications, 1973Abstract Electron transport particles from M. phlei contain at least 3 different active forms of cytochrome b, one reduced by NADH, with a λmax at 563 nm (bN563), and the other two reduced by either succinate or NADH, with λmax at 559 and 563 nm (bS559) and (bS563).
N S, Cohen +3 more
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Archives of Biochemistry and Biophysics, 1986
A new membrane-bound b-type cytochrome, cytochrome b-558, was removed from chromatophore membranes of photosynthetically grown Rhodopseudomonas sphaeroides strain R-26 by deoxycholate-cholate extraction. The cytochrome was purified by ammonium sulfate fractionation and ion-exchange chromatography.
K, Iba, K, Takamiya
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A new membrane-bound b-type cytochrome, cytochrome b-558, was removed from chromatophore membranes of photosynthetically grown Rhodopseudomonas sphaeroides strain R-26 by deoxycholate-cholate extraction. The cytochrome was purified by ammonium sulfate fractionation and ion-exchange chromatography.
K, Iba, K, Takamiya
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Mitochondrial Cytochrome b 560
1987Cytochrome b 560 the succinate-ubiquinone (Q) reductase region of the mitochondrial electron transfer chain was first reported by Davis et al. (1,2). In spite of the detection of cytochrome b 560 in various succinate -Q1 reductase (3,4), and Complex II (5–7) preparations, this cytochrome has often been regarded as a contaminant of the denatured ...
Chang-An Yu, Linda Yu
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1986
Publisher Summary This chapter describes the purification of neutrophilic leukocytes from peripheral blood, the isolation of their membranes that are enriched in the cytochrome, the preparation of a solubilized oxidase, and the purification of the cytochrome itself.
Anthony W. Segal +3 more
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Publisher Summary This chapter describes the purification of neutrophilic leukocytes from peripheral blood, the isolation of their membranes that are enriched in the cytochrome, the preparation of a solubilized oxidase, and the purification of the cytochrome itself.
Anthony W. Segal +3 more
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Assembly of chloroplast cytochromes b and c
Biochimie, 2000The synthesis of holocytochromes in plastids is a catalyzed process. Several proteins, including plastid CcsA, Ccs1, possibly CcdA and a thioredoxin, plus at least two additional Ccs factors, are required in sub-stoichiometric amounts for the conversion of apocytochromes f and c(6) to their respective holoforms.
S S, Nakamoto, P, Hamel, S, Merchant
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Interaction of cytochrome b₅ and cytochrome c
2010The interaction and kinetics of electron transfer between cytochrome b₅ and cytochrome c, two well characterised soluble electron transfer proteins, have been investigated by three techniques. First, fluorescence quenching experiments were done with cytochrome b₅ and porphyrin cytochrome c, a fluorescent analogue of cytochrome c.
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Some photoreactions of isolated cytochrome b-559
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1977Cytochrome b-559 was isolated from spinach and the alga Bumilleriopsis filiformis (Xanthophyceae) and characterized by functional properties: (a) It was active as electron acceptor in a diaphorase system using NADPH as donor and ferredoxin and ferredoxin-NADP reductase as redox proteins.
H J, Lach, H, Böhme, P, Böger
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1955
Publisher Summary Cytochrome b of mammalian tissue is a hemoprotein which in the reduced (ferrous) form has absorption bands centered at 564 mμ (α), 530 mμ (β), and 430 mμ (γ). In heart muscle extracts which contain both an active succinic dehydrogenase and cytochrome oxidase, the addition of succinate causes reduction of cytochrome b and aeration ...
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Publisher Summary Cytochrome b of mammalian tissue is a hemoprotein which in the reduced (ferrous) form has absorption bands centered at 564 mμ (α), 530 mμ (β), and 430 mμ (γ). In heart muscle extracts which contain both an active succinic dehydrogenase and cytochrome oxidase, the addition of succinate causes reduction of cytochrome b and aeration ...
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1975
Publisher Summary Type b cytochromes are electron-carrying proteins, which contain protoheme IX as the prosthetic group. The position of α band of their absorption spectra in the ferrous state ranges from 554 to 566 nm. By the pyridine treatment they give the pyridine-protohemochrome with its α band at 556 nm.
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Publisher Summary Type b cytochromes are electron-carrying proteins, which contain protoheme IX as the prosthetic group. The position of α band of their absorption spectra in the ferrous state ranges from 554 to 566 nm. By the pyridine treatment they give the pyridine-protohemochrome with its α band at 556 nm.
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