State of aggregation of detergent-solubilized sarcoplasmic reticulum adenosine triphosphatase investigated by high-performance liquid chromatography
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,General Medicine,Biochemistry,Analytical Chemistry
Reference18 articles.
1. The Effect of Delipidation on the Adenosine Triphosphatase of Sarcoplasmic Reticulum. Electron Microscopy and Physical Properties
2. Retention of enzyme activity by detergent-solubilized sarcoplasmic Ca2+ion-activated ATPase
3. Properties of deoxycholate solubilized sarcoplasmic reticulum Ca2+ ion-dependent ATPase
4. Effect of the lipid environment on protein motion and enzymatic activity of sarcoplasmic reticulum calcium ATPase.
5. The functional unit of calcium-plus-magnesium-ion-dependent adenosine triphosphatase from sarcoplasmic reticulum. The aggregational state of the deoxycholate-solubilized protein in an enzymically active form
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1. Integral Membrane Proteins;Journal of Chromatography Library;2000
2. Protein-protein interaction of detergent-solubilized Ca2+-ATPase during ATP hydrolysis analyzed by low-angel laser light scattering photometry coupled with high-performance gel chromatography;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1990-10
3. Mizellare Beeinflussung analytischer Reaktionen und Prozesse;Analytiker-Taschenbuch;1990
4. Detergent structure and Associated Lipid as Determinants in the Stabilization of Solubilized Ca2+-ATPase from Sarcoplasmic Reticulum;Journal of Biological Chemistry;1989-03
5. Site-directed cross-linking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis.;Journal of Biological Chemistry;1988-05
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