INVESTIGADORES
DELFINO Jose Maria
artículos
Título:
Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling
Autor/es:
VILLAMIL GIRALDO AM; CASTELLO PR; GONZÁLEZ FLECHA FL; MOELLER JV; DELFINO JM; ROSSI JPFC
Revista:
FEBS LETTERS
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2006 vol. 580 p. 607 - 612
ISSN:
0014-5793
Resumen:
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 (á-subunit) and 5.6 mol PC / mol protein for the Na,K-ATPase (beta-subunit).
