A phospholamban protein phosphatase associated with canine cardiac sarcoplasmic reticulum was isolated and characterized as a 46,000 Mr globular protein capable of dephosphorylating phospholamban.
Canine cardiac sarcoplasmic reticulum vesicles contain intrinsic phospholamban protein phosphatase activity, which is also effective in dephosphorylating phosphorylase a. The phosphatase associated with sarcoplasmic reticulum membranes was solubilized with Triton X-100 and subjected to chromatography on Mono Q HR 5/5 and polylysine-agarose. A single peak of phosphatase activity was eluted from each column and it was coincident for both phospholamban and phosphorylase a, used as substrates. Thermal denaturation of the enzyme resulted in progressive and coincident loss of both phospholamban and phosphorylase a phosphatase activities. Enzymic activity was partially inhibited by protein phosphatase inhibitor 1. Migration of the enzyme during sucrose density gradient ultracentrifugation corresponded to a globular protein with an apparent Mr of 46,000. This enzyme preparation could dephosphorylate both the calcium-calmodulin-dependent as well as the cAMP-dependent sites on phospholamban. Thus, dephosphorylation of phospholamban by this sarcoplasmic reticulum-associated phosphatase may participate in modulating sarcoplasmic reticulum function in cardiac muscle.
Kranias et al. (Fri,) reported a other. Biochemical characterization was evaluated on Phosphatase activity and enzyme characterization. A phospholamban protein phosphatase associated with canine cardiac sarcoplasmic reticulum was isolated and characterized as a 46,000 Mr globular protein capable of dephosphorylating phospholamban.
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