Disease relevance of 2BR

• In this work, we demonstrate that the substitution of Coomassie Brilliant Blue for bromophenol blue in two-dimensional electrophoresis (2-DE) buffers improves the focusing of whole proteins from Pseudomonas aeruginosa [1].
• Reductively debrominating strains of Propionigenium maris from burrows of bromophenol-producing marine infauna [2].
• Rhodococcus sp. RB1 nitrate reductase had an apparent molecular mass of 142 kDa and used NADH and reduced bromophenol blue or viologens as electron donors, independently of the presence of salt [3].
• Complex formation between Chromatium vinosum ferric cytochrome c' and bromophenol blue [4].
• Investigations of immunoblots using Borrelia burgdorferi antigen demonstrated that a band, migrating faster than the bromophenol blue front in sodium dodecyl sulfate-gel electrophoresis, reacted strongly with sera containing anti-Borrelia burgdorferi antibodies preferentially of the IgG class [5].

High impact information on 2BR

• The formation of 2-bromophenol and bromobenzene-2,3-dihydrodiol was increased more than 10-fold in incubations of hepatocytes from beta-naphthoflavone-treated rats, as compared to those of hepatocytes from untreated rats, but recovery of 4-bromocatechol was unchanged [6].
• 6. Neither NADH nor NADPH was effective as an electron donor, but reduced Methyl Viologen (apparent Km 998 microM) and reduced Bromophenol Blue (apparent Km 158 microM) were effective [7].
• The pH dependence of binding of bromophenol blue and of bromocresol purple, which has a higher pKa than bromophenol blue, indicated that binding was dependent on protonation of a protein residue with a pKa of 2 [8].
• Titration of bound bromophenol blue indicated that the deprotonated dye was bound to the strong site with approximately 20-fold greater affinity than the protonated dye [8].
• This method was also used to isolate a form of enterotoxin that has a mobility, relative to bromophenol blue tracking dye, of 0.87 to 0.90 in 7% acrylamide gels [9].

Chemical compound and disease context of 2BR

• The interactions of catechol (substrate), 2-hydroxy-pyridine-N-oxide (substrate analogue), and 2-bromophenol (inhibitor) with the extradiol cleaving catechol-2,3-dioxygenase from Pseudomonas putida mt-2 have been monitored through X-ray absorption spectroscopy (XAS) [10].

Biological context of 2BR

• In the case of chymotrypsin, bromophenol blue was found to activate the enzyme catalyzed hydrolysis of p-nitrophenyl acetate, and a rate process was observed with the temperature jump which could be attributed to a conformational change of the indicator-protein complex [11].
• Detection and characterization of a dehalogenating microorganism by terminal restriction fragment length polymorphism fingerprinting of 16S rRNA in a sulfidogenic, 2-bromophenol-utilizing enrichment [12].
• Dose-dependent pharmacokinetics and hepatobiliary transport of bromophenol blue in the beagle [13].
• Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue [14].
• Kinetics and thermodynamics of bromophenol blue adsorption by a mesoporous hybrid gel derived from tetraethoxysilane and bis(trimethoxysilyl)hexane [15].

Anatomical context of 2BR

• Liver microsomes converted o-bromophenol to 2-bromohydroquinone and covalently bound material, whereas kidney and lung microsomes metabolized o-bromophenol less rapidly [16].
• Incubation of either o-bromophenol or 2-bromohydroquinone with rat liver microsomes and 0.25 mM 35S-glutathione (GSH) gave rise to several isomeric 35S-GSH conjugates [17].
• The prostatic cytosol incubated with 3H-dihydrotestosterone (3H-DHT) revealed radioactive areas with the following average electrophoretic mobilities relative to Bromophenol Blue (Rf): 0.195, 0.285, 0.815, 0.910 [18].
• Some goblet cells were positive for Bromophenol Blue but numerous cells were unstained; thus many proteins and possibly lipids may be conjugated with sugars [19].
• Effect of indomethacin on the permeability of blood-brain and blood-csf barriers to Evans blue, bromophenol blue and horseradish peroxidase (HRP) was studied by administering the drug through right internal carotid artery, right external jugular vein and through intraperitoneal route in rats [20].

Associations of 2BR with other chemical compounds

• The pH indicators bromothymol blue, bromophenol blue, and phenol red were used to monitor pH changes associated with the monomer-dimer interaction [11].
• 2-Bromohydroquinone was identified as a metabolite of both bromobenzene and o-bromophenol in the rat in vivo and in vitro [16].
• Terminal restriction fragment length polymorphism analysis of reverse-transcribed 16S rRNA during periods of community flux was used as a tool to delineate the roles of the members of a 2-bromophenol-degrading, sulfate-reducing consortium [12].
• Spectroscopic studies indicated greater ionization of citric acid and bromophenol blue in solution and the solid state with increasing initial solution pH, as expected [21].
• In this study, the "pH memory" is explored by comparing the extent of protonation of sulfonephthalein probe molecules, bromophenol blue, bromocresol green, and chlorophenol red, in aqueous solution in the pH range of 3.4-6.0 and in the resulting freeze-dried amorphous matrix (lyophile) containing trehalose and sodium citrate buffer [22].

Gene context of 2BR

• Bromophenol red as a probe of lysozyme-active site environment: a temperature-jump study [23].
• Two-way ANOVA showed that only the 30% S. siliquastrum-containing feed significantly (p < 0.05) increased the total bromophenol content in the fish flesh with time [24].
• The isolated proteins (PAP I-a, PAP I-b and PAP II) were homogeneous in various methods including 7.5% and 20% gel electrophoresis or gel chromatography, and share, in the extract, 85% of the total of the acidic proteins that migrate with the bromophenol blue marker in 7.5% gels [25].

Analytical, diagnostic and therapeutic context of 2BR

• The interaction of bromophenol blue and related dyes with bovine neurophysin-I was studied by equilibrium dialysis and gel filtration, absorption and circular dichroism spectroscopy, and analytical ultracentrifugation [8].
• By contrast, the apomyoglobin-protoporphyrin IX complex does not react with Bromophenol Blue. 6. Optical-rotatory-dispersion measurements show that the laevorotation of apomyoglobin is increased towards that of metmyglobin in the presence of haemin and protoporphyrin IX [26].
• Densitometry of gelled-in Bromophenol Blue showed that these pore gradients exhibited a linear central segment and were reproducible [27].
• A stable coculture was established which contained predominantly 2BP-48 and a second Desulfovibrio-like bacterium (designated BP212 based on terminal restriction fragment length polymorphism fingerprinting) that was capable of dehalogenating 2-bromophenol to phenol [12].
• TGI-I and II gave a band that migrated faster than bromophenol blue marker dye, but they did not pass through an ultrafiltration membrane with an Mr cutoff of 5,000 [28].

References