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Journal Article

Tryptophan fluorescence of sarcoplasmic reticulum ATPase. A fluorescence quench study

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;

/persons/resource/persons124261

Gaugler,  Hans
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0005273685904262/pdf?md5=10570ef09de9db3a23f421a835dbeb12&pid=1-s2.0-0005273685904262-main.pdf
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https://doi.org/10.1016/0005-2736(85)90426-2
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Citation

Lüdi, H., Hasselbach, W., & Gaugler, H. (1985). Tryptophan fluorescence of sarcoplasmic reticulum ATPase. A fluorescence quench study. Biochimica et Biophysica Acta: BBA, 814(1), 120-124. doi:10.1016/0005-2736(85)90426-2.


Cite as: https://hdl.handle.net/21.11116/0000-0005-9889-5
Abstract
The calcium-dependent change in the tryptophan fluorescence intensity of the sarcoplasmic reticulum Ca2+- and Mg2+-ATPase was investigated using different quenching reagents. It is demonstrated that only those compounds which are bound to the enzyme (i.e., 1-(9,10-dibromomyristoyl)-sn-2-glycerophosphorylcholine and 1-(9,10-dibromostearoyl)-sn-glycero-3-phosphorylcholine) are able to decrease the amplitude of the fluorescence decrement observed after removal of calcium ions. From the position of the bromine atom within the lysophosphatidylcholines, it is concluded that the tryptophan residues involved are located in the hydrophobic part of the ATPase molecule and are in contact with the hydrocarbon chains of the phospholipids.