High impact information on CYTB

• Affinity-purified rabbit anti-neutrophil cytochrome b light or heavy chain antibodies were used to immunocytochemically and biochemically localize cytochrome b in neutrophils and eosinophils [1].
• However, the system showed high O2(-)-generating activity of 31.8 mol/s/mol of cytochrome b558 (52.5% of the original O2(-)-generating activity of the solubilized membranes) in the presence of a nitro blue tetrazolium (NBT) reductase fraction that was separated from the cytochrome b fraction by heparin-Sepharose chromatography [2].
• Furthermore, mRNA transcripts from these nuclear genes encoding mitochondrial proteins did not increase to the same extent as mRNA transcripts of mitochondrial genes such as cytochrome b, which increased 5.9-fold after 21 days of stimulation [3].
• When cardiac muscle and Type I (red, oxidative) skeletal muscle were compared to Type II (white, glycolytic) skeletal muscle, mitochondrial DNA, mitochondrial ribosomal RNA, and cytochrome b mRNA, each increased in direct proportion to increases in oxidative capacity [4].
• We demonstrated an upregulation of the U6 snRNA binding protein Lsm5, cytochrome b, an expressed sequence tag, and the actin-depolymerizing factor cofilin2 mRNA in collateral arteries 24h after femoral ligation [5].

Biological context of CYTB

• Digestion with eight enzymes of a 1120-bp fragment comprising most of the cytochrome b gene resolved 38 different haplotypes [6].
• Phylogeography of the European rabbit (Oryctolagus cuniculus) in the Iberian Peninsula inferred from RFLP analysis of the cytochrome b gene [6].
• To this end, we have collected DNA sequence data from a 702-bp region of the mitochondrial cytochrome b gene and reconstructed the evolutionary history (via parsimony, neighbor joining, and maximum likelihood) of 11 species of Lepus, focusing on North American taxa [7].
• Cytochrome b phylogeny of North American hares and jackrabbits (Lepus, lagomorpha) and the effects of saturation in outgroup taxa [7].
• Spectroscopic analysis of the cytochromes of the respiratory chain shows that only cytochrome b is present in chondrocytes from cartilage, cytochromes c, c1, and a.a3 being undetectable as compared with the typical spectrum found in a primary cell culture on day 4 [8].

Anatomical context of CYTB

• Furthermore, when the phenotypic characteristics of Type II skeletal muscle were altered by electrical stimulation in vivo, mitochondrial DNA, mitochondrial rRNA, and cytochrome b mRNA also increased proportionately with increases in oxidative capacity [4].
• Differential responses of mitochondrial respiration and cytochrome b redox states in the presence and absence of magnesium indicate that with magnesium present, heart mitochondria retain the ability to phosphorylate ADP after calcium uptake [9].

Associations of CYTB with chemical compounds

• Furthermore, the cytochrome b component of the NADPH oxidase was found in greater quantities within wound neutrophils [10].

References