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.About:
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.read more
Citations
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Journal ArticleDOI
Glyoxal-induced modification enhances stability of hemoglobin and lowers iron-mediated oxidation reactions of the heme protein: An in vitro study.
TL;DR: In vitro investigation of the in vitro effect of the reactive α-oxoaldehyde on the heme protein hemoglobin revealed modification of arginine residues of HbA0 to hydroimidazolone adducts, suggesting AGE-induced modifications appear to be associated with the observed changes of theheme protein.
Journal ArticleDOI
Trifluoperazine is more effective than chlorpromazine in releasing oxygen from haemoglobin and myoglobin.
TL;DR: The extent of oxygen release from two heme proteins, haemoglobin and myoglobin, have been studied in the presence of trifluoperazine and chlorpromazine (5–1000 μM).
Journal ArticleDOI
Probing the toxic mechanism of bisphenol A with acid phosphatase at the molecular level
TL;DR: This work suggested the structures and functions of acid phosphatase were both affected by BPA, and BPA could enhance the fluorescence intensity, change the structure, and cause an increased hydrophobicity of acidosphatase.
Journal ArticleDOI
Functional inhibition of redox regulated heme proteins: A novel mechanism towards oxidative stress induced by homocysteine.
TL;DR: In this article, the effect of homocysteine (Hcy) toxicity on proteins with iron as cofactors was investigated and it was shown that redox regulated heme proteins might be primarily involved in the Hcy toxicity and associated oxidative stress.
Journal ArticleDOI
Interactions of chlorpromazine with milk proteins.
Jaya Bhattacharyya,Kali P. Das +1 more
TL;DR: Far UV Circular dichroic studies reveal that CPZ increases the secondary structure of the major β-sheeted protein, β-lactoglobulin possibly by increasing the relative contact orders (non-local contacts) within the residues.
References
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Journal ArticleDOI
Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle.
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
N. J. De Mol,R.W. Busker +1 more
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.
Related Papers (5)
Thermodynamics of protein association reactions: forces contributing to stability
Philip D. Ross,S. Subramanian +1 more