Steroid-protein interactions studied by fluorescence quenching

Attallah, N.A.; Lata, Gene F.

doi:10.1016/0005-2795(68)90154-2

Cited by 54 publications

(15 citation statements)

References 35 publications

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“…Absorption and emission spectra were taken, the average value of emission and absorption intensity was measured. For each hormone (testosterone, androsterone, dehydroepiandrosterone (DHEA) and dehydroepiandrosterone sulfate (DHEAS)), the binding constant Kb was calculated by the method [10] as well as the stoichiometric concentration of a bound hormone Bmax and a change in free energy of the system G  . The interaction of hormone and erythrocyte membrane is described by the equation…”

Section: Fluorescence Analysis Of Erythrocyte Shadowsmentioning

confidence: 99%

Mesomechanics and Thermodynamics of Nanostructural Transitions in Biological Membranes Under the Action of Steroid Hormones

Панин¹

2012

Thermodynamics - Fundamentals and Its Application in Science

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Section: Fluorescence Analysis Of Erythrocyte Shadowsmentioning

confidence: 99%

Mesomechanics and Thermodynamics of Nanostructural Transitions in Biological Membranes Under the Action of Steroid Hormones

Панин¹

2012

Thermodynamics - Fundamentals and Its Application in Science

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“…Absorption and emission spectra were taken, the average value of emission and absorption intensity was measured. For each hormone (cortisol, adrenaline or noradrenaline), the binding constant K b was calculated by the method (Attallah & Lata, 1968) as well as the stoichiometric concentration of a bound hormone B max and a change in free energy of the system ∆G. The interaction of cortisol and erythrocyte membrane is described by the equation…”

Section: Fluorescence Analysis Of Erythrocyte Shadowsmentioning

confidence: 99%

Thermodynamics and Mesomechanics of Nanostructural Transitions in Biological Membranes as Liquid Crystals

Панин¹

2011

Application of Thermodynamics to Biological and Materials Science

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Biological membranes play a key role in structural-functional organization of any cells. Membranes constitute 65% of the cell dry weight, of them 40% belong to lipids and 60% to simple and conjugate proteins. Membranes separate cell into functional units (divisions); as a result, cell operates as a complicated factory in miniature. Besides, membranes integrate the operation of cell as a whole. Cell is an open system. It steadily exchanges weight, energy and information with the environment. This process also involves the biological (cell) membranes. All biological membranes are liquid-crystalline structures. They consist of phospholipids bilayer, with simple and conjugate proteins immersed in it. These are various membranebound enzymes, transmembrane carriers (of glucose, Na + and K + ions, and others), and hormone receptors that serve as signal mechanisms of the cell. Structure-forming bonds in liquid crystals are represented by covalent and hydrogen bonds, hydrophobic and electrostatic interactions. These are the low-energy binding: covalent bonds -50-100 kcal/mol, hydrogen bonds -about 6 kcal/mol. Between fatty acid tails of phospholipids there is a large amount of water dipoles. Such structure of the membrane provides high mobility of its structural components relative to each other. Membranes are reinforced by cholesterol molecules, which strengthen the hydrophobic interactions. Such membrane responds to external action as a cooperative system. Changes in structure and function of erythrocyte membranes in vivoThese studies were performed with thirteen participants of a Russia-Canadian transarctic ski transition "Dickson (Russia) -North Pole -Canada" within the polar day period (Observation…, 1992). In this section, we present the results of analysis of the structuralfunctional characteristics of erythrocyte membranes within a long (three-month) stay of humans in arctic deserts. MethodologyErythrocyte 'shadows' were obtained at Dickson, the North Pole, and in Ottawa. The objectives of this investigation were to study the viscosity, specific electrical conductivity,

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“…Quenching is thought to occur when there is a close association of the tryptophan group of HSA and the drug which allows a radiationless energy transfer from the tryptophan to the drug to dissipate the tryptophan's absorbed energy. Thus the quenching of the native fluorescence of HSA by the binding of tolmetin suggests that tolmetin is bound at the tryptophan site (site I) association constant determined at pH 7.4 from the following equation (Attallah & Lata 1968):…”

Section: R E S U L T S a N D Discussionmentioning

confidence: 99%

The effects of pH, calcium and chloride ions on the binding of tolmetin to human serum albumin: circular dichroic, dialysis and fluorometric measurements

Matsuyama

Sen

Perrin

1987

Journal of Pharmacy and Pharmacology

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The binding of the non‐steroidal anti‐inflammatory drug, tolmetin (1‐methyl‐5‐p‐toluoylpyrrole‐2‐acetic acid) to human serum albumin (HSA) has been shown by circular dichroism, fluorescence and equilibrium dialysis to be dependent on the N‐B conformational change of the albumin. The influence of calcium and chloride ions on the interaction was also investigated using the same techniques. Experiments suggested that calcium ions increased the binding constant of tolmetin to HSA whereas chloride ions decreased it. The displacement study showed that tolmetin caused a significant increase in the affinity of diazepam to HSA whereas it decreased the binding of warfarin to HSA. Tolmetin seems to cause an allosteric change in the diazepam binding site in spite of it sharing a primary site with warfarin.

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Steroid-protein interactions studied by fluorescence quenching

Cited by 54 publications

References 35 publications

Mesomechanics and Thermodynamics of Nanostructural Transitions in Biological Membranes Under the Action of Steroid Hormones

Mesomechanics and Thermodynamics of Nanostructural Transitions in Biological Membranes Under the Action of Steroid Hormones

Thermodynamics and Mesomechanics of Nanostructural Transitions in Biological Membranes as Liquid Crystals

The effects of pH, calcium and chloride ions on the binding of tolmetin to human serum albumin: circular dichroic, dialysis and fluorometric measurements

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