[The effect of a structural modification in the membrane proteins on the lipid-protein interaction in human erythrocyte membranes].
The effect of resonance energy transfer from excited tryptophan residues of proteins towards the pyrene molecules which took place in a close association, has been used to study lipid-protein interaction in human erythrocyte membranes. Diamide, N-ethylmaleimide, and t-butyl hydroperoxide were utilized to modify membrane proteins. The disturbance of membrane protein architecture induced by N-ethylmaleimide, and t-butyl hydroperoxide resulted in the increase of the mobility of pyrene molecules being present in the microenvironment of membrane proteins. In the bulk lipid matrix no detectable changes were observed. The influence of the reagents on the erythrocyte membranes was controlled using merocyanine 540 and spin-probe techniques.
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D001798:Blood Proteins / Q000187:drug effects / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D004347:Drug Interactions; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D005456:Fluorescent Dyes; D006801:Humans; D015227:Lipid Peroxidation / Q000187:drug effects; D008560:Membrane Fluidity / Q000187:drug effects; D008563:Membrane Lipids / Q000097:blood*; D008565:Membrane Proteins / Q000097:blood* / Q000187:drug effects; D011721:Pyrenes; D013050:Spectrometry, Fluorescence; D013113:Spin Labels; D013329:Structure-Activity Relationship
D001798:Blood Proteins; D005456:Fluorescent Dyes; D008563:Membrane Lipids; D008565:Membrane Proteins; D011721:Pyrenes; D013113:Spin Labels; C030984:pyrene
Vliianie strukturnoĭ modifikatsii membrannykh belkov na lipid-belkovoe vzaimodeĭstvie v membranakh éritrotsitov cheloveka.