Excimer formation in pyrenemaleimide-labeled sarcoplasmic reticulum ATPase

Excimer formation in pyrenemaleimide-labeled sarcoplasmic reticulum ATPase

The authors' interpretation of the excimer peak in N-(3-pyrene)maleimide-labeled ATPase was based on the following observations: (a) N-(3-pyrene)maleimide binds preferentially to the fast reacting thiol group, and (b) the excimer peak was decreased after the addition of nonsolubilizing amounts...

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Veröffentlicht in:Biophysical journal 1987-03, Vol.51 (3), p.513-514
Hauptverfasser: Lüdi, H., Hasselbach, W.
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Triphosphatases - metabolism
Letter
Maleimides - pharmacology
Muscles - enzymology
Sarcoplasmic Reticulum - enzymology
skeletal muscle
Spectrometry, Fluorescence - methods
Sulfhydryl Reagents - pharmacology
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Zusammenfassung:The authors' interpretation of the excimer peak in N-(3-pyrene)maleimide-labeled ATPase was based on the following observations: (a) N-(3-pyrene)maleimide binds preferentially to the fast reacting thiol group, and (b) the excimer peak was decreased after the addition of nonsolubilizing amounts of detergent, such as myristoylglycero-phosphocholine or C sub(12)E sub(8).
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(87)83374-X