Purification of phospholamban, a 22,000-dalton protein from cardiac sarcoplasmic reticulum that is specifically phosphorylated by cyclic AMP-dependent protein kinase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
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2. [27] Isolation of proteins of the sarcoplasmic reticulum
3. The Stimulation of Calcium Transport in Cardiac Sarcoplasmic Reticulum by Adenosine 3′:5′-Monophosphate-dependent Protein Kinase
4. Adenosine 3′,5′-monophosphate-dependent phosphorylation of a 6000 and A 22000 dalton protein from cardiac sarcoplasmic reticulum
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1. Purified, Reconstituted Cardiac Ca2+-ATPase Is Regulated by Phospholamban but Not by Direct Phosphorylation with Ca2+/Calmodulin-dependent Protein Kinase;Journal of Biological Chemistry;1996-06
2. Characterization of the molecular form of cardiac phospholamban;Molecular and Cellular Biochemistry;1994
3. Functional reconstitution of the cardiac sarcoplasmic reticulum Ca2(+)-ATPase with phospholamban in phospholipid vesicles.;Journal of Biological Chemistry;1990-01
4. Distances between functional sites in cardiac sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase. Inter-Ianthanide energy transfer;European Journal of Biochemistry;1988-12
5. cAMP-dependent protein phosphorylation of membrane proteins in the parotid gland, platelets and liver. Comparison of a 22-kDa phosphoprotein from rat parotid microsomes (protein III) with phosphoproteins of similar molecular size from platelet and liver membranes;European Journal of Biochemistry;1988-07
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