Enzyme kinetics and substrate stabilization of detergent-solubilized and membraneous (Ca2+ + Mg2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions.
Open Access
- 1 March 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (5) , 1912-1920
- https://doi.org/10.1016/s0021-9258(19)85969-0
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- Properties of a delipidated, detergent-activated calcium(2+)-activated ATPaseBiochemistry, 1978
- Fluorescence energy transfer between Ca2+ transport ATPase molecules in artificial membranesBiochemistry, 1977
- Kinetics and Regulation of Sarcoplasmic Reticulum ATPaseEuropean Journal of Biochemistry, 1977
- Properties of deoxycholate solubilized sarcoplasmic reticulum Ca2+ ion-dependent ATPaseBiochemistry, 1976
- Interaction of calcium and magnesium in activating and inhibiting the nucleoside triphosphatase of sarcoplasmic reticulum vesiclesBiochimica et Biophysica Acta (BBA) - Enzymology, 1975
- ATP and Ca2+ binding by the Ca2+ pump protein of sarcoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- Isolation of sarcoplasmic reticulum by zonal centrifugation and purification of Ca2+-pump and Ca2+-binding proteinsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- Isoleucyl‐tRNA SynthetaseEuropean Journal of Biochemistry, 1971
- Relaxing factor and the relaxation of muscleProgress in Biophysics and Molecular Biology, 1964
- Measurement of protein-binding phenomena by gel filtrationBiochimica et Biophysica Acta, 1962