Document Actions
Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling
Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling
5378
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 [(125)I]TID-PC/16 was incorporated into mixtures of dimyristoyl phosphatidylcholine (DMPC) and each enzyme with the aid of the nonionic detergent C(12)E(10). 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 (alpha-subunit) and 5.6 mol PC/mol protein for the Na,K-ATPase (beta-subunit).
Villamil Giraldo AM, Castello PR, González Flecha FL, Moeller JV, Delfino JM, Rossi JP
FEBS letters
2006-01-23 00:00
580
2
607-12
Animals,Calcium-Transporting ATPases,Cation Transport Proteins,Detergents,Humans,Light,Lipids,Molecular Structure,Na(+)-K(+)-Exchanging ATPase,Phosphatidylcholines,Plasma Membrane Calcium-Transporting ATPases,Rabbits,Sarcoplasmic Reticulum Calcium-Transporting ATPases,Staining and Labeling,Swine,Cation Transport Proteins,Detergents,Lipids,Phosphatidylcholines,Na(+)-K(+)-Exchanging ATPase,Calcium-Transporting ATPases,Plasma Membrane Calcium-Transporting ATPases,Sarcoplasmic Reticulum Calcium-Transporting ATPases
Instituto de Química y Fisicoquímica Biológicas, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín 956.C1113AAD, Buenos Aires, Argentina.
FEBS Lett.
0014-5793
10.1016/j.febslet.2005.12.078
S0014-5793(05)01563-2
0
False
16412439
