Characterization of structural unit of phospholamban by amino acid sequencing and electrophoretic analysis.
The partial amino acid sequence of phospholamban from canine cardiac sarcoplasmic reticulum was determined by sequence analysis of the peptides obtained from the protein cleaved by cyanogen bromide and with TPCK-trypsin. The sequence determined initiated with N alpha-acetylated methionine followed by 44 amino acid residues intervening two unidentified residues. This polypeptide would represent a structural unit (protomer) of phospholamban. Analysis of temperature-dependent conversion of phospholamban from 26 kDa to lower molecular weight form (6 kDa) suggested that phospholamban holoprotein is composed of five identical protomers.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002135:Calcium-Binding Proteins; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008970:Molecular Weight; D009206:Myocardium / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D012519:Sarcoplasmic Reticulum / Q000032:analysis; D000099211:Phospholamban
D000596:Amino Acids; D002135:Calcium-Binding Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D000099211:Phospholamban