Results 251 to 260 of about 50,722 (302)

Crystalline Cytochrome b 5

Nature, 1959
CYTOCHROME c and b 5 are the only cytochromes isolated from animal tissues in purified soluble forms which are reducible by soluble flavoprotein. Further studies on the enzymatic and chemical properties of cytochrome b 5 are badly needed.
I, RAW, W, COLLI
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Cytochrome b and photosynthetic sulfur bacteria

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
Chromatophores isolated from the purple sulfur bacterium Chromatium and the green sulfur bacterium Chlorobium exhibit absorbance changes in the cytochrome alpha-band region consistent with the presence of a b-type cytochrome. Cytochrome content determined by reduced minus oxidized difference spectra and by heme photochemically active ...
D B, Knaff, B B, Buchanan
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High-energy Forms of Cytochrome b

Nature, 1970
SUB-MITOCHONDRIAL particles prepared from horse or ox heart contain two species of cytochrome b in equal amounts, one (bi) affected by antimycin and the other (b) not affected1–3. In addition to its well known inhibitory effect on the respiratory chain, acting between cytochromes b and c1, antimycin brings about an increased reduction of the total ...
E C, Slater, C P, Lee, J A, Berden, H J, Wegdam   +3 more
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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, 1973
Abstract 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, E, Bogin, T, Higashi, A F, Brodie   +3 more
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A new membrane-bound b-type cytochrome, cytochrome b-558, from photosynthetically grown Rhodopseudomonas sphaeroides

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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Mitochondrial Cytochrome b 560

1987
Cytochrome 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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[21] Cytochrome b-245

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, Angela M. Harper, Andrew R. Cross, Owen T.G. Jones   +3 more
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Assembly of chloroplast cytochromes b and c

Biochimie, 2000
The 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

2010
The 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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