Disease relevance of Bromobimane

• When Mycobacterium smegmatis was treated with the alkylating agent monobromobimane (mBBr), the cellular mycothiol was converted to its bimane derivative (MSmB) [1].
• Using the 5,5'-dithiobis(2-nitrobenzoic acid)-reduction assay and monobromobimane revelation we showed that TrxTa is specifically reduced by wheat NADP:thioredoxin reductase (NTR), and not by E. coli NTR [2].
• The effects of monobromobimane on neuronal cell death in the hippocampus after transient global cerebral ischemia in rats [3].
• The purpose of the present study was to determine whether monobromobimane (MBM) was a possible protective agent against neuronal cell death after transient global ischemia and the swelling of isolated hippocampal mitochondria [3].
• These results are discussed in terms of the dynamic fluxes in monobromobimane protein thiols during fractionation and the applicability of this noninvasive method to studies of the mechanism(s) of toxicity of reactive xenobiotics and the role(s) of protein thiols in normal cellular function [4].

High impact information on Bromobimane

• Tissue extracts incubated with reduced thioredoxin are treated with a fluorescent probe (monobromobimane) to label sulfhydryl groups [5].
• Monobromobimane labeling and protein-free thiol titration revealed significantly less extensive oxidation in the cauda epididymis when compared to that in the wild type [6].
• Cytochalasin D (CD) and monobromobimane (MB) enhanced agglutination and prevented the inhibitory action of ADP on bovine vWf-induced platelet agglutination [7].
• We find that two mutants, I72C and S251C, when labeled with the small, solvent-sensitive fluorophore monobromobimane, exhibit spectral changes only upon binding light-activated, phosphorylated rhodopsin [8].
• We have determined the distribution of glutathione between different chemical states in rat liver microsomes by labeling with the thiol-specific label monobromobimane and subsequent separation by reversed phase high performance liquid chromatography [9].

Biological context of Bromobimane

• S-Glutahionylation of the 20 S core was demonstrated in vitro by GSH-biotin incorporation and by decreased alkylation with monobromobimane [10].
• Probing the active site of alpha-class rat liver glutathione S-transferases using affinity labeling by monobromobimane [11].
• Although they are slower to react, the sterically bulkier reagents, monobromobimane and menadione, effectively alkylate the most susceptible ER zinc finger cysteine sulfhydryl groups [12].
• The presence of the N-acetylcysteine moiety was indicated by formation of N-acetylcysteine-monobromobimane during acid hydrolysis of the monobromobimane derivative of U17 [13].
• Aim of this study was to investigate the effects of the resin monomer BisGMA on the glutathione concentration (monobromobimane assay) and apoptosis (Annexin V/PI-assay) of cultured primary human gingival fibroblasts [14].

Anatomical context of Bromobimane

• The thiol redox status of cultured human bronchial fibroblasts has been characterized at various growth conditions using thiol-reactive monobromobimane, with or without the combination of dithiotreitol, a strong reducing agent [15].
• METHODS: Human mesangial cells were treated with 15dPGJ2 and intracellular thiol status was monitored by the fluorescent thiol probe monobromobimane (MBB) [16].
• Fluorescently labeled G-protein was extracted from bleached rod outer segments (ROS) reacted with several sulfhydryl reagents: N-(1-pyrenyl)maleimide (P), monobromobimane (B), 7-(diethylamino)-3-(4-maleimidylphenyl)-4-methylcoumarin (C), and N-(4-anilino-1-naphthyl)maleimide (A) [17].
• Dynamics of the thiol status of rat spermatozoa during maturation: analysis with the fluorescent labeling agent monobromobimane [18].
• Bromobimane crosslinking studies in oligomycin-sensitive ATPase from beef heart mitochondria. Mr 31 000 protein crosslinked [19].

Associations of Bromobimane with other chemical compounds

• Cells were extracted in the presence of monobromobimane (mBBr) to convert thiols to fluorescent derivatives, which were analyzed by high-pressure liquid chromatography [20].
• Here we describe a procedure for the detection and relative quantitation of MBB-labeled cysteines using fluorescence and mass spectrometric analyses, which allow determination of free cysteine content and unambiguous identification of MBB-modified cysteine residues [21].
• Cystine was measured as cysteine after reduction with sodium borohydride and derivatization with monobromobimane, followed by separation with automated HPLC and fluorescence detection [22].
• Intact spermatozoa were labeled with monobromobimane, with or without pretreatment with dithiothreitol [18].
• Selective inhibition of the mitochondrial permeability transition pore at the oxidation-reduction sensitive dithiol by monobromobimane [23].

Gene context of Bromobimane

• Monobromobimane and N-dansylaziridine labeled GPIb beta but not GPIb alpha in intact platelets [24].
• The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with [14C]iodoacetate and monobromobimane [25].
• Two types of PC analyses are currently used, i.e., acid extraction and separation on HPLC with either precolumn derivatization (pH 8.2) with monobromobimane (mBBr) or postcolumn derivatization (pH 7.8) with Ellman's reagent [5, 5'-dithiobis(2-nitrobenzoic acid), DTNB] [26].
• Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi [27].
• A highly sensitive and specific assay for Escherichia coli thioredoxin was developed using the thiol-specific reagent monobromobimane [28].

Analytical, diagnostic and therapeutic context of Bromobimane

• Precolumn derivatization with bromobimane and reversed-phase HPLC were performed automatically by a sample processor [29].
• While peptide mass profiles are severely altered in protein samples prelabeled with monobromobimane, successful identification of proteins by peptide mass profiling using matrix-assisted laser desorption/ionization mass spectrometry was easily performed after protein detection with SYPRO Ruby Protein Gel stain [30].
• Sperm analysis by flow cytometry using the fluorescent thiol labeling agent monobromobimane [31].
• Two-dimensional polyacrylamide gel electrophoresis of proteins labeled with the fluorophore monobromobimane prior to first-dimensional isoelectric focusing: imaging of the fluorescent protein spot patterns using a cooled charge-coupled device [32].
• The nuclei were separated from the incubation medium by centrifugation through silicone oil, and the thiols were determined in the nuclear pellet and in the incubation buffer by labeling with monobromobimane and HPLC [33].

References