Purification of phospholamban, a 22,000-dalton protein from cardiac sarcoplasmic reticulum that is specifically phosphorylated by cyclic AMP-dependent protein kinase

Very low concentrations of the detergent, deoxycholate, have been used to isolate two functionally interesting proteins from canine cardiac sarcoplasmic reticulum. These two proteins are phospholamban, a 22,000-dalton protein, specifically phosphorylated by adenosine 3':5'-monophosphate-de...

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Bibliographic Details
Published in:The Journal of biological chemistry 1982-04, Vol.257 (8), p.4501-4506
Main Authors: Bidlack, J M, Ambudkar, I S, Shamoo, A E
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
adenosinetriphosphatase
Animals
Ca(2+) Mg(2+)-ATPase
Calcium-Binding Proteins - isolation & purification
Calcium-Binding Proteins - metabolism
Calcium-Transporting ATPases - metabolism
Cattle
Cyclic AMP - pharmacology
Deoxycholic Acid - pharmacology
Dogs
heart
Heart Ventricles - metabolism
Kinetics
Microsomes - metabolism
Myocardium - metabolism
phospholamban
Phosphorylation
purification
sarcoplasmic reticulum
Sarcoplasmic Reticulum - enzymology
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Summary:Very low concentrations of the detergent, deoxycholate, have been used to isolate two functionally interesting proteins from canine cardiac sarcoplasmic reticulum. These two proteins are phospholamban, a 22,000-dalton protein, specifically phosphorylated by adenosine 3':5'-monophosphate-dependent protein kinase, and the (Ca super(2+) + Mg super(2+))-ATPase, the major protein of the sarcoplasmic reticulum, responsible for the active transport of calcium.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)34751-3