Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling
Stoichiometry of lipid-protein interaction assessed by hydrophobic photolabeling
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DOI：
10.1016/j.febslet.2005.12.078
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发表时间：
2006-01-23
期刊：
影响因子：
3.5
通讯作者：
Rossi, JPFC
中科院分区：
文献类型：
--
作者：
Giraldo, AMV;Castello, PR;Rossi, JPFC
本文对P型家族的三种ATP酶：质膜钙泵（PMCA）、肌浆网钙泵（SERCA）和Na，K-ATP酶的脂环组成进行了比较研究。借助于非离子去污剂C12 E10，将光活化磷脂酰胆碱类似物[I-125]TID-PC/16掺入二肉豆蔻酰磷脂酰胆碱（DMPC）和每种酶的混合物中。光解后，评估标记反应的程度以确定脂质：蛋白质化学计量：PMCA为17，SERCA为18，Na，K-ATP酶（α亚基）为24，Na，K-ATP酶（β亚基）为5.6 mol PC/mol蛋白质。(c)2005年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
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 [I-125]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 (alpha-subunit) and 5.6 mol PC/mol protein for the Na,K-ATPase (beta-subunit). (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.