Erythrosin Isothiocyanate Selectively Labels Lysine464 within an ATP-Protectable Binding Site on the Ca-ATPase in Skeletal Sarcoplasmic Reticulum Membranes
Author:
Affiliation:
1. Department of Biochemistry, Cell and Molecular Biology, University of Kansas, Lawrence, Kansas 66045-2106
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi980275f
Reference56 articles.
1. Mechanism of Calcium Transport
2. Teaching active transport at the turn of the twenty-first century: recent discoveries and conceptual changes
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2. Phosphorylation by cAMP-Dependent Protein Kinase Modulates the Structural Coupling between the Transmembrane and Cytosolic Domains of Phospholamban;Biochemistry;2003-08-20
3. Differential Inactivation of Na,K-ATPase by Erythrosin Isothiocyanate;Annals of the New York Academy of Sciences;2003-04
4. Inactivation of Na,K-ATPase Following Co(NH3)4ATP Binding at a Low Affinity Site in the Protomeric Enzyme Unit;Journal of Biological Chemistry;2003-04
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