Journal ArticleDOI
Studies on the interaction of chlorpromazine with haemoglobin.
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TLDR
The interaction of chlorpromazine (CPZ), a widely used antipsychotic tranquillizer, with the allosteric protein haemoglobin, has been studied by different methods and the possible nature of the binding site of the protein has been discussed on the basis of the information obtained from fluorescence measurements.About:
This article is published in International Journal of Biological Macromolecules.The article was published on 1990-10-01. It has received 12 citations till now. The article focuses on the topics: Cooperativity.read more
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Interaction of chlorpromazine with myoglobin and hemoglobin: A comparative study
TL;DR: 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.
Journal ArticleDOI
Structural organisations of hemoglobin and myoglobin influence their binding behaviour with phenothiazines
TL;DR: Binding modalities of chlorpromazine and trifluoperazine, two widely used antipsychotic phenothiazine drugs with hemoglobin and myoglobin have been studied to understand how the quaternary, tertiary and secondary structural organisations of the proteins regulate the binding process.
Journal ArticleDOI
Protoporphyrin IX-induced structural and functional changes in human red blood cells, haemoglobin and myoglobin.
TL;DR: Spectrophotometric studies reveal that protoporphyrin IX interacts with haemoglobin and myoglobin forming ground state complexes, which may have a role in establishing efficacy of therapeutic uses of porphyrins as well as in elucidating their mechanisms of action as therapeutic agents.
Journal ArticleDOI
Studies on the interaction of hematoporphyrin with hemoglobin.
TL;DR: Spectrophotometric and spectrofluorimetric studies reveal that an interaction occurs between hemoglobin and hematoporphyrin, a photosensitizing drug used in photodynamic therapy, and appears to be predominantly electrostatic and enthalpy-driven in the lower range of porphyrIn concentration.
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Interaction of porphyrins with heme proteins--a brief review.
TL;DR: The effect of porphyrins on heme proteins should be given due consideration in elucidating the details of the mechanism of p Morphyrin actions in therapy.
References
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Journal ArticleDOI
Binding of chlorpromazine, phenytoin and aspirin to the erythrocytes and lipoproteins in whole human blood.
TL;DR: The results suggest that the amphiphilic drugs with relatively high hydrophobicity may be bound to the blood cells, mainly to erythrocytes, to considerable extents when administered clinically, and also that their binding to plasma lipoproteins may not be negligible.