Fluorometric Study of the solubilized Ca2+ -ATPase of sarcoplasmic reticulum
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(80)81179-3/fullpdf
Reference10 articles.
1. Fluorescence studies of the sarcoplasmic reticulum calcium pump
2. Transient kinetics of sarcoplasmic reticulum Ca2++Mg2+ ATPase studied by fluorescence
3. Mechanism of the sarcoplasmic reticulum calcium pump. Fluorometric study of the phosphorylated intermediates
4. Change in the Ultraviolet Spectrum of Solubilized Ca2+-Dependent ATPase from Sarcoplasmic Reticulum due to Binding with Ca2+Ions1
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1. Use of Glycerol-Containing Media To Study the Intrinsic Fluorescence Properties of Detergent-Solubilized Native or Expressed SERCA1a;Biochemistry;2008-10-24
2. Crystal Structure of D351A and P312A Mutant Forms of the Mammalian Sarcoplasmic Reticulum Ca2+-ATPase Reveals Key Events in Phosphorylation and Ca2+ Release;Journal of Biological Chemistry;2008-05
3. Synthetic Monoacylphospholipids as Reactivators of the Calcium-Dependent ATPase of Enzymatically Delipidated Sarcoplasmic Membranes;European Journal of Biochemistry;2005-03-03
4. Purification of Heterologous Sarcoplasmic Reticulum Ca2+-ATPase Serca1a Allowing Phosphoenzyme and Ca2+-Affinity Measurements;Protein Expression and Purification;2001-07
5. Cancellation of the cooperativity of Ca2+ binding to sarcoplasmic reticulum Ca2+-ATPase by the non-ionic detergent dodecylmaltoside;European Journal of Biochemistry;1994-07
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