Inactivation of detergent-solubilized sarcoplasmic reticulum ATPase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb13890.x/fullpdf
Reference28 articles.
1. Properties of a delipidated, detergent-activated calcium(2+)-activated ATPase
2. Enzyme kinetics and substrate stabilization of detergent-solubilized and membraneous (Ca2+ + Mg2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions.
3. The Influence of Detergents on the Ca2+-and Mg2+-Dependent Adenosine Triphosphatase of the Sarcoplasmic Reticulum
4. Kinetic characterization of detergent-solubilized sarcoplasmic reticulum ATPase
5. Monomeric solubilized sarcoplasmic reticulum Ca pump protein: demonstration of Ca binding and dissociation coupled to ATP hydrolysis.
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2. Purification of Heterologous Sarcoplasmic Reticulum Ca2+-ATPase Serca1a Allowing Phosphoenzyme and Ca2+-Affinity Measurements;Protein Expression and Purification;2001-07
3. A kinetic study of an unstable enzyme measured through coupling reactions. Application to the self-inactivation of detergent-solubilized Ca2+-ATPase from sarcoplasmic reticulum;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1993-11
4. Existence of High- and Low-Affinity Vanadate-Binding Sites on Ca2+-ATPase of the Sarcoplasmic Reticulum1;The Journal of Biochemistry;1991-12
5. Stabilization of detergent-solubilized Ca2+-ATPase by poly(ethylene glycol);Biochimica et Biophysica Acta (BBA) - Biomembranes;1989-09
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