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Journal ArticleDOI

Interaction of chlorpromazine with myoglobin and hemoglobin: A comparative study

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TLDR
Thermodynamic analysis revealed that binding of CPZ to hemoglobin was exothermic, whereas binding to myoglobin was endothermic with a high entropic contribution, suggesting that CPZ binding toMyoglobin is hydrophobic in nature.
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This article is published in Biochemical Pharmacology.The article was published on 1994-06-01. It has received 68 citations till now. The article focuses on the topics: Myoglobin & Binding constant.

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Citations
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Journal ArticleDOI

Interaction of pyrene-end-capped poly(ethylene oxide) with bovine serum albumin and human serum albumin in aqueous buffer medium: a fluorometric study.

TL;DR: The photophysical behavior of a hydrophobically tailored water-soluble polymer, pyrene-end-capped poly(ethylene oxide) (PYPY), has been studied in aqueous buffered bovine serum albumin (BSA) and human serumalbumin (HSA) media and the binding interaction has been shown to have a prominent role on the steady state fluorescence anisotropy of the two emission bands.
Journal ArticleDOI

Probing the binding of 8-Acetyl-7-hydroxycoumarin to human serum albumin by spectroscopic methods and molecular modeling.

TL;DR: Interaction of 8-Acetyl-7-hydroxycoumarin with human serum albumin (HSA) at pH 7.40 has been investigated at 291, 301 and 310 K, respectively, employing the steady fluorescence, circular dichroism (CD) and molecular modeling methods to determine the quenching mechanism and binding constants.
Journal ArticleDOI

Study of the interaction of deoxynivalenol with human serum albumin by spectroscopic technique and molecular modelling.

TL;DR: Molecular modelling revealed that a DON–protein complex was stabilised by hydrophobic forces and hydrogen bonding, potentially useful for elucidating the toxigenicity of DON when combined with biomolecular function effect, transmembrane transport, toxicological testing and the other experiments.
Journal ArticleDOI

Methylglyoxal modification enhances the stability of hemoglobin and lowers its iron-mediated oxidation reactions: An in vitro study.

TL;DR: In the present study, the in vitro effect of methylglyoxal (MG) on the heme protein hemoglobin (HbA0) (100μm) after incubation for one week at 25°C is investigated.
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Glyoxal administration induces formation of high molecular weight aggregates of hemoglobin exhibiting amyloidal nature in experimental rats: An in vivo study

TL;DR: Glyoxal was found to modify Arg-30β and Arg-31α of rat hemoglobin to hydroimidazolone adducts, which appear to induce amyloid-like aggregation of hemoglobin in rats, which may be physiologically significant.
References
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Journal ArticleDOI

Evidence for cooperative binding of chlorpromazine with hemoglobin: equilibrium dialysis, fluorescence quenching and oxygen release study.

TL;DR: Binding of chlorpromazine with human hemoglobin has been studied by equilibrium dialysis and fluorescence quenching and results revealed that the binding was positively cooperative with overall affinity constant K = 3.8 x 10(3) M-1.
Book ChapterDOI

Preparation of myoglobins.

TL;DR: This chapter presents procedures for the isolation of intracellular oxygen-binding proteins of tissues, called “tissue hemoglobins” in the widest sense, which are monomers or dimers having a minimum molecular weight of 18,000 with similar optical spectra and chemical reactivity.
Journal ArticleDOI

Irreversible binding of the chlorpromazine radical cation and of photoactivated chlorpromazine to biological macromolecules

TL;DR: The irreversible binding of chlorpromazine radical cation (CPZ+.) and photoactivated chlor Promazine ( CPZ) to calf thymus DNA in vitro and bacterial macromolecules in intact bacterium cells was investigated and the consequences of covalent binding for the cytotoxicity and genotoxicity of CPZ+.
Journal ArticleDOI

Protein-ligand interactions: interaction of nitrosamines with nicotinic acetylcholine receptor.

TL;DR: Scatchard analysis indicates that all four ligands are true agonists of the receptor exhibiting positive cooperative binding with the existence of more than one class of binding site.
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