These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [The effect of a structural modification in the membrane proteins on the lipid-protein interaction in human erythrocyte membranes].
    Author: Gorbunov NV.
    Journal: Biull Eksp Biol Med; 1993 Nov; 116(11):488-91. PubMed ID: 8312536.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]