Steady state determination of sarcoplasmic reticulum ATPase intermediates. Their acid lability.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference35 articles.
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Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Calcium additional to that bound to the transport sites is required for full activation of the sarcoplasmic reticulum Ca-ATPase from skeletal muscle;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1998-10
2. Direct demonstration of an acid-labile phosphoenzyme in the cycle of the sarcoplasmic reticulum Ca2+-dependent adenosinetriphosphatase;Biochimica et Biophysica Acta (BBA) - Biomembranes;1990-11
3. Demonstration of the simultaneous activation of Ca2+-independent and Ca2+-dependent ATPases from rat skeletal muscle microsomes;Biochimica et Biophysica Acta (BBA) - Biomembranes;1988-04
4. Equilibrium and steady state thermodynamics of active transport systems studied on simple models simulating Ca2+ transport through sarcoplasmic reticulum membranes;Journal of Theoretical Biology;1986-05
5. Phosphorylation by ATP of sarcoplasmic reticulum ATPase in the absence of calcium.;Journal of Biological Chemistry;1983-03
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