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Journal Article

Excimer formation of ATPase from sarcoplasmic reticulum labeled with N-(3-pyrene)maleinimide

MPS-Authors
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Lüdi,  Hans
Max Planck Institute for Medical Research, Max Planck Society;

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Hasselbach,  Wilhelm
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1983.tb07108.x
(Any fulltext)

https://doi.org/10.1111/j.1432-1033.1983.tb07108.x
(Any fulltext)

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Citation

Lüdi, H., & Hasselbach, W. (1983). Excimer formation of ATPase from sarcoplasmic reticulum labeled with N-(3-pyrene)maleinimide. European Journal of Biochemistry, 130(1), 5-8. doi:10.1111/j.1432-1033.1983.tb07108.x.


Cite as: https://hdl.handle.net/21.11116/0000-0003-6B95-D
Abstract
Sarcoplasmic reticulum ATPase from fast skeletal muscle was labeled in native vesicles with N-(3-pyrene)maleinimide. At labeling ratios larger than 1 mol pyrenemaleinimide/2.5 mol ATPase significant amounts of excimers are detected. Excimer concentration decreases at low, non-solubilizing amounts of detergents (0.2 mg X mg protein-1) and completely disappears after solubilization of the membranes. These results exclude that excimers are formed due to 'double-labeling' of one ATPase molecule. It is concluded that the ATPase exists as an oligomer within the membrane of native vesicles.