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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

Novel binding studies of human serum albumin with trans-feruloyl maslinic acid

TL;DR: 3-trans-feruloyl maslinic acid, a non-fluorescent derivative of Tetracera asiatica, is extracted from the medicinal plant and found that FMA binds strongly in different places with hydrogen bonding at IB domain of Arg 114, Leu 115 and Asp 173.
Journal ArticleDOI

Daidzein interaction with human serum albumin studied using optical spectroscopy and molecular modeling methods

TL;DR: In this paper, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) and molecular modeling methods were used to characterize optical properties of the Daidzein-HSA complex and to gain information on the binding mechanism at molecular level.
Journal ArticleDOI

Spectroscopic investigation on the interaction of 3,7-dihydroxyflavone with different isomers of human serum albumin.

TL;DR: The results indicated that 3,7-diHF, in anionic form, was bound within the hydrophobic pockets of the subdomain IIA of HSA (site I), and stabilised mainly by electrostatic force and ionic interactions.
Journal ArticleDOI

Spectroscopic and molecular modeling of the binding of meso-tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin

TL;DR: The binding of meso -tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin has been investigated by the combination of fluorescence, UV–vis absorption, Fourier transform infrared, circular dichroism spectroscopies and molecular modeling, suggesting that the colorant can partially insert into the site II of subdomain IIIA via hydrophobic and hydrogen bonding interactions.
Journal ArticleDOI

Methylglyoxal-induced modifications of hemoglobin: structural and functional characteristics.

TL;DR: The modified protein was found to be more effective than HbA(0) in H(2)O(2)-mediated iron release and oxidative damages involving Fenton reaction and may enhance oxidative stress and associated complications, particularly in diabetes mellitus with increased level of MG.
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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