1984
DOI: 10.1007/bf02453343
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Spin labelling of human erythrocytes with nitroxide radicals

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Cited by 4 publications
(2 citation statements)
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“…The covalent bindings between these spin labels and the internal RBC -SH group prevents their return to the plasma and changes the RBC into label cells. [28][29] Nitroxide radical ESR signal was recorded at 20 8C using an X-band ESR Spectrometer Bruker ECS 106 with an ESR aqueous flat cell. The spectrometer settings for the nitroxide radicals were: field center 3440 G, sweep width 80 G, microwave frequency 9.7 GHz, microwave power 10 mW, time constant 327.68 ms, modulation frequency 50 KHz, modulation amplitude 0.205 G, and resolution 1024 points.…”
Section: Methodsmentioning
confidence: 99%
“…The covalent bindings between these spin labels and the internal RBC -SH group prevents their return to the plasma and changes the RBC into label cells. [28][29] Nitroxide radical ESR signal was recorded at 20 8C using an X-band ESR Spectrometer Bruker ECS 106 with an ESR aqueous flat cell. The spectrometer settings for the nitroxide radicals were: field center 3440 G, sweep width 80 G, microwave frequency 9.7 GHz, microwave power 10 mW, time constant 327.68 ms, modulation frequency 50 KHz, modulation amplitude 0.205 G, and resolution 1024 points.…”
Section: Methodsmentioning
confidence: 99%
“…Both labels have been extensively used to study the molecular dynamics of many proteins [17][18][19][20][21] because the spin label can be considered as an additional amino acid residue [22]. In this way, the ESR spectrum of the spin label covalently bound to the protein can reflect either the motion of the macromolecule itself or some residual motion of the label with respect to the whole macromolecule.…”
Section: Introductionmentioning
confidence: 99%