Properties of a phosphorylated intermediate of the Ca,Mg-activated ATPase of microsomal vesicles from uterine smooth muscle
- 1 August 1984
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 232 (2) , 616-623
- https://doi.org/10.1016/0003-9861(84)90581-2
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
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- Demonstration of the phosphorylated intermediates of the Ca2+-transport ATPase in a microsomal fraction and in a (Ca2+ + Mg2+)-ATPase purified from smooth muscle by means of calmodulin affinity chromatographyBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982
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- Ca2+ Uptake, Ca2+-ATPase Activity, Phosphoprotein Formation and Phosphate Turnover in a Microsomal Fraction of Smooth MuscleEuropean Journal of Biochemistry, 1981
- Characterization of cell membrane and sarcoplasmic reticulum from bovine uterine smooth muscleArchives of Biochemistry and Biophysics, 1980
- Characterization of Cardiac Sarcoplasmic Reticulum ATP‐ADP Phosphate Exchange and Phosphorylation of the Calcium Transport Adenosine TriphosphataseEuropean Journal of Biochemistry, 1976
- Role of Calcium Binding by Sarcoplasmic Reticulum in the Contraction and Relaxation of Uterine Smooth MuscleThe Journal of general physiology, 1969