Separation of the tryptic fragments of sarcoplasmic reticulum ATPase with high performance liquid chromatography. Identification of the calcium binding site.
The four tryptic fragments of the Ca2+- and Mg2+-dependent ATPase from sarcoplasmic reticulum were separated on a TSK-G 4000 SW preparative high performance liquid chromatography column in the presence of sodium dodecyl sulfate. Using atomic absorption spectroscopy, the analysis of the protein peaks demonstrated that the calcium binding sites with high affinities are located in the smallest fragment (A2; 25 kDa).
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000818:Animals; D001665:Binding Sites; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D010446:Peptide Fragments / Q000302:isolation & purification*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013054:Spectrophotometry, Atomic; D014357:Trypsin / Q000378:metabolism*
D010446:Peptide Fragments; D014357:Trypsin; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D002118:Calcium