Limited proteolysis of human erythrocyte Ca2+-ATPase in membrane-bound form. Identification of calmodulin-binding fragments.
Water-soluble and membrane-bound calmodulin-binding polypeptides formed upon limited proteolysis of erythrocyte ghosts were isolated by means of affinity chromatography. Immune blotting revealed that all isolated fragments originated from Ca2+-ATPase. Among the fragments obtained those having formed an acylphosphate intermediate were identified. The N-terminal residue of purified intact Ca2+-ATPase was shown to be blocked (probably acylated).
Emelyanenko
E I
EI
Shakhparonov
M I
MI
Modyanov
N N
NN
D000596:Amino Acids / Q000032:analysis; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism*
D000596:Amino Acids; D002147:Calmodulin; D010446:Peptide Fragments; D000252:Calcium-Transporting ATPases