Characterization of the aflatoxin B1-binding site of rat albumin.

  title={Characterization of the aflatoxin B1-binding site of rat albumin.},
  author={Heini W. Dirr and Johannes C. Schabort},
  journal={Biochimica et biophysica acta},
  volume={913 3},
8 Citations
Aflatoxin B1 Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study
The study confirms the static nature of fluorescence quenching and finds the stoichiometry of binding sites was found to be unity, and the competing capability of warfarin for AFB1 was higher than ibuprofen as calculated from site marker displacement assay.
Species Differences of Serum Albumins: I. Drug Binding Sites
It is proposed herein that mammalian serum albumins used in this study contain specific drug binding sites: Rabbit and rat albumins contain a drug binding site, corresponding to site I on human albumin, and dog albumin contains a specific drugbinding site corresponding tosite II on the human album in molecule.
Effect of phenylbutazone on serum protein binding and disposition of sulfadimethoxine in human and rabbit
Findings indicated that in the case of rabbit, phenylbutazone indirectly reduced the in vivo binding of SDM to serum through the displacing effect of N4-AcSDM.
Products of Spontaneous Conjugation of Aflatoxins with Bovine Serum Albumin: Immunochemical Properties
Products of spontaneous conjugation of aflatoxins B1, G1, and G2 with bovine serum albumin (BSA) were shown to interact with antibodies against aflatoxins. Solid-phase BSA conjugates inhibited the
Use of cyclodextrins as modifiers of fluorescence in the detection of mycotoxins
An attempt to extend the use of cyclodextrins to the detection of labelled T-2 toxin is presented and it is revealed that heptakis (2,6-di-O-methyl)-β-cyclodextrin (DIMEB), in particular, enhanced T2-Pyr fluorescence.
2 . 4 . 1 Albumin and other carrier proteins
Soluble proteins make up 6.4–8.3% of plasma by weight [1], a value comparable to their concentration in cell water [2]. Many plasma proteins are synthesized by the liver. Their concentrations may
A Review on Biological Control and Metabolism of Aflatoxin
  • H. Mishra, C. Das
  • Biology, Medicine
    Critical reviews in food science and nutrition
  • 2003
Biological control methods with special emphasis on in vivo and in vitro enzymatic detoxification of aflatoxin have been reviewed and future areas of research involving large-scale enzyme detoxification and modified atmosphere storage are discussed.
Effect of phenylbutazone on serum protein binding and pharmacokinetic behavior of sulfadimethoxine in rabbits, dogs and rats.
Findings indicate that in rabbits, PBZ indirectly reduces the in vivo binding of SDM through the interaction of PBZ with N4-AcSDM, which appears to be negligible in dogs.


Drug-binding properties of rat alpha-foetoprotein. Specificities of the phenylbutazone-binding and warfarin-binding sites.
Rat alpha-foetoprotein strongly binds the drugs warfarin and phenylbutazone, as does albumin, but the binding sites for the two drugs seemed to be different, and a negative modulatory effect is exerted between the two sites.
Relations between high-affinity binding sites of markers for binding regions on human serum albumin.
The present findings support the proposal of four separate primary binding sites for warfarin, digitoxin (and salicylate), diazepam and Phenol Red.
The characterization of two specific drug binding sites on human serum albumin.
The binding of a number of fluorescent probe molecules to human serum albumin has been studied and changes in probe fluorescence were shown to be a result of competitive displacement by drugs.
Drug-binding properties of rat alpha 1-foetoprotein. Binding of warfarin, phenylbutazone, azapropazone, diazepam, digitoxin and cholic acid.
The alpha 1-FP led to an increased affinity for warfarin, phenylbutazone and azapropazone without a change in the measured number of sites, indicating competition for binding at this site by (an) endogenous ligand(s).
Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone.
This paper reports a variety of experimental observations which strongly support the assumption that the warfarin binding site, or site I of human serum albumin, is better described as the
Quantitative assessment of the competitive binding of anionic ligands to albumin.
It is concluded that fluorescence is not a quantitative indicator of ANS binding to albumin and is not suitable for determination of competitive interactions.
Fluorimetric analysis of the binding of warfarin to human serum albumin. Equilibrium and kinetic study.
Activation parameters obtained in the kinetic experiments correspond very well with the thermodynamic parameters calculated from the equilibrium study, validating the fluorescence approach to the equilibrium studies.
Relations between high-affinity binding sites for L-tryptophan, diazepam, salicylate and Phenol Red on human serum albumin.
Binding of L-tryptophan, diazepam, salicylate and Phenol Red to defatted human serum albumin was studied by ultrafiltration at pH 7.0. All ligands bind to one high-affinity binding site with