Distinction of the roles of the two high-affinity calcium sites in the functional activities of the Ca2+-ATPase of sarcoplasmic reticulum
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1984.tb08390.x/fullpdf
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1. Disruption of energy transduction in sarcoplasmic reticulum by trypsin cleavage of (Ca2++Mg2+)-ATPase
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4. The binding of nucleotides and bivalent cations to the calcium-and-magnesium ion-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum
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1. Uncoupling of Occlusion From ATP Hydrolysis Activity in Sarcoplasmic Reticulum (Ca2++Mg2+)-ATPase;Membrane Biochemistry;1993-01
2. Participation of a non-covalent phosphointermediate in ATP hydrolysis by the sarcoplasmic reticulum Ca2+-transport ATPase;European Journal of Biochemistry;1990-09
3. Identification of a Spectroscopic Marker for the Ca2+-Binding Site of (Ca2++ Mg2+)-ATPase of Sarcoplasmic Reticulum in the Occluded State;Membrane Biochemistry;1990-01
4. Effect of protease digestion on the secondary structure of sarcoplasmic reticulum Ca2+-ATPase as seen by FT-i.r. spectroscopy;International Journal of Biochemistry;1990-01
5. Mechanism of Ca2+ Translocation as Studied by the use of Detergent-Solubilized and Membrane Preparations of Sarcoplasmic Reticulum Ca2+-ATPase;Bioelectrochemistry III;1990
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