Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: DrugBank:EXPT00841 (Cibacron Blue)
 478 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Anthraquinone dyes (ADs), originally developed for the textile industry, are useful nucleotide-specific ligands for the purification of proteins by affinity techniques. Their specific feature is to mimic the adenine nucleotides ATP, ADP, NAD, NADH, which enables them to interact with the nucleotide-binding sites of enzymes such as dehydrogenases, kinases and ATPases. In the present study, the interactions and/or inhibitory effects of seven ADs, including Cibacron Blue F3G-A, Remazol Brilliant Blue R, on the activity of lactate dehydrogenase (LDH) were investigated. The ADs used in this paper could be divided into two groups: (i) AD1-AD3 which do not contain a triazine moiety; (ii) AD4-AD7 which contain the triazine moiety. Enzyme kinetics and zonal affinity chromatography were used for the characterization of the interaction affinity between the dye and LDH. Enzyme kinetic measurements were carried out at three different pH values: 6.5, 7.5 and 8.5. The relationship between physical and chemical properties of ADs (e.g., acid-basic properties, three dimensional structure of the respective dyes) and their interaction efficiency with LDH was studied. LDH activity was inhibited by all ADs, excluding AD1 (precursor of the blue dyes) and inhibition was always competitive. Similarity in the mutual position of the acidic and basic groups in NADH and the respective AD molecule was found to be a crucial factor for influencing the inhibitory action of the substance. The existence of ADs in the protonated form should be considered as another factor, important for the ADs inhibitory action on this enzyme.
 ...
PMID:Interaction of lactate dehydrogenase with anthraquinone dyes: characterization of ligands for dye-ligand chromatography. 979 15

A specific feature of anthraquinone dyes (AD) is to mimic the adenine nucleotides ATP, ADP, NAD and NADH, enabling them to act as ligands in interaction with nucleotide-binding sites of several enzymes and receptors. In the present study, the interactions and/or inhibitory effects of eight AD, including Cibacron Blue 3G-A (Reactive Blue 2), Procion Blue MX-R (Reactive Blue 4) and Remazol Brilliant Blue R (Reactive Blue 19) on the activity of (Na(+)/K(+))-ATPase were investigated. The AD used in this paper could be divided into two groups: i) AD1-AD4 that do not contain the triazine moiety; ii) AD5-AD8 that contain the triazine moiety. Interaction affinity between the respective dye and (Na+/K+)-ATPase was characterized by means of enzyme kinetics. All AD, excluding AD1 and AD2 (which were practically ineffective) exerted effective competitive inhibition to the (Na(+)/K(+))-ATPase activity. Present study is devoted to elucidation of relationship between the inhibitory efficacy of AD against (Na(+)/K(+))-ATPase activity, their acid-basic properties and their three dimensional structure. From the results obtained, the following conclusions could be driven: 1. Similarities in the mutual position of positively and negatively charged parts of ATP and AD are responsible for their interaction with ATP-binding site of (Na(+)/K(+))-ATPase. This may be documented by fact that mutual position of 1-aminogroup of anthraquinone and -SO3(-) group of benzenesulphonate part of respective AD plays crucial role for inhibition of this enzyme. Distances of these two groups on all effective AD were found to be similar as the distance of the 6-aminogroup of adenine and the second phosphate group on ATP molecule. This similarity could be responsible for biomimetic recognition of AD in ATP-binding loci of (Na(+)/K(+))-ATPase. 2. The affinity of AD to ATP binding site of (Na(+)/K(+))-ATPase increases with increasing values of molar refractivity, i. e., with increasing molecular volume and polarizability.
 ...
PMID:Inhibition of (Na(+)/K(+))-ATPase by Cibacron Blue 3G-A and its analogues. 1735 35