Transient kinetic analysis of turnover-dependent fluorescence of 2‘,3‘-O-(2,4,6-trinitrophenyl)-ATP bound to Ca2+-ATPase of sarcoplasmic reticulum.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference41 articles.
1. Occurrence and role of tightly bound adenine nucleotides in sarcoplasmic reticulum of rabbit skeletal muscle.
2. Alterations in the structure of the ribose moiety of ATP reduce its effectiveness as a substrate for the sarcoplasmic reticulum ATPase.
3. Energy coupling and uncoupling of active calcium transport by sarcoplasmic reticulum membranes
4. Proton inactivation of Ca2+ transport by sarcoplasmic reticulum.
5. Effect of K+ on phosphorylation of the sarcoplasmic reticulum ATPase by either Pi or ATP.
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4. Catalysis of an ATP analogue untethered and tethered to lysine 492 of sarcoplasmic reticulum Ca(2+)-ATPase.;Journal of Biological Chemistry;1994-08
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