A Remarkably Stable Phosphorylated Form of Ca2+-ATPase Prepared from Ca2+-loaded and Fluorescein Isothiocyanate-labeled Sarcoplasmic Reticulum Vesicles

After the nucleotide binding domain in sarcoplasmic reticulum Ca2+-ATPase has been derivatized with fluorescein isothiocyanate at Lys-515, ATPase phosphorylation in the presence of a calcium gradient, with Ca2+ on the lumenal side but without Ca2+ on the cytosolic side, results in the formation of a...

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Veröffentlicht in:	The Journal of biological chemistry 2001-02, Vol.276 (8), p.5795-5803
Hauptverfasser:	Champeil, Philippe, Henao, Fernando, Lacapère, Jean-Jacques, McIntosh, David B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological Transport, Active Calcium - metabolism Calcium-Transporting ATPases - metabolism Cell Polarity Cytosol Enzyme Stability Fluorescein-5-isothiocyanate Fluorescence Models, Chemical Organophosphates - metabolism Phosphates - metabolism Phosphoproteins - metabolism Sarcoplasmic Reticulum - enzymology Spectrophotometry
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