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• W1528657116 abstract "Monoclonal antibodies raised against canine cardiac sarcoplasmic reticulum phospholamban were used to study the structure-function relationship between phospholamban and the sarcoplasmic reticulum (SR) (Ca(2+)-Mg2+)-ATPase (Suzuki, T., and Wang, J. H. (1986) J. Biol. Chem. 261, 7018-7023). Additional monoclonal antibodies are characterized further. When five of these monoclonal antibodies were assessed for their ability to affect SR Ca2+ uptake three of these antibodies had no effect on SR Ca2+ uptake, whereas the other two monoclonals were able to stimulate SR Ca2+ uptake to levels similar to those caused by phosphorylation of phospholamban at different calcium concentrations. Using synthetic peptides corresponding to various portions of phospholamban in a competitive binding assay, it was possible to map the epitope site of monoclonals which stimulate the (Ca(2+)-Mg2+)-ATPase activity to phospholamban residues 7-16. These results implicate phospholamban residues 7-16 in the regulation of the (Ca(2+)-Mg2+)-ATPase." @default.
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• W1528657116 date "1991-06-01" @default.
• W1528657116 modified "2023-10-03" @default.
• W1528657116 title "Phospholamban regulation of cardiac sarcoplasmic reticulum (Ca(2+)-Mg2+)-ATPase. Mechanism of regulation and site of monoclonal antibody interaction" @default.
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• W1528657116 doi "https://doi.org/10.1016/s0021-9258(18)99158-1" @default.
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