Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling

Citations of this article
Mendeley users who have this article in their library.


Here we undertook a comparative study of the composition of the lipid annulus of three ATPases pertaining to the P-type family: plasma membrane calcium pump (PMCA), sarcoplasmic reticulum calcium pump (SERCA) and Na,K-ATPase. The photoactivatable phosphatidylcholine analogue [ 125I]TID-PC/16 was incorporated into mixtures of dimyristoyl phosphatidylcholine (DMPC) and each enzyme with the aid of the nonionic detergent C12E10. After photolysis, the extent of the labeling reaction was assessed to determine the lipid:protein stoichiometry: 17 for PMCA, 18 for SERCA, 24 for the Na,K-ATPase (α-subunit) and 5.6 mol PC/mol protein for the Na,K-ATPase (β-subunit). © 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.




Giraldo, A. M. V., Castello, P. R., Flecha, F. L. G., Moeller, J. V., Delfino, J. M., & Rossi, J. P. F. C. (2006). Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling. FEBS Letters, 580(2), 607–612.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free