[125I]Iodonaphtylazide labeling selectively a cysteine residue in the F0 of the ATP‐synthase from E. coli is unsuitable for topographic studies of membrane proteins

FEBS Letters

Friedl, P.²  Hoppe, J.²  Jørgensen, B.B¹ 

[1] Dept. of Microbiology, The Technical University of Denmark, Building 221, DK-2800 Lyngby-Copenhagen, Denmark;Dept. of Cytogenetics, GBF, Gesellschaft für Biotechnologische Forschung mbH., Mascheroder Weg 1, D-3300 Braunschweig, FRG

关键词: Hydrophobic labeling;    Nitrene;    Membrane protein;    Proton channel;   

DOI  :  10.1016/0014-5793(83)80974-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ATP synthase from E. coli was reacted with the hydrophobic photolabel [¹²⁵I]iodonaphtylazide. Subunit b in the F₀-part was selectively labelled. Label was traced back to the single cysteine₂₁ in subunit b. Thus the reactive intermediate of INA generated by photolysis had a high preference for nucleophiles. Due to this high selectivity the detection of membrane spanning peptide segments by labelling with INA is not reliable.

【 授权许可】

Unknown