Oligomerisation of sarcoplasmic reticulum Ca2+-ATPase monomers from skeletal muscle.
The fast-twitch SERCA1 isoform of the sarcoplasmic reticulum Ca(2+)-ATPase was purified to homogeneity and conjugated to peroxidase. The SERCA1 probe showed high affinity binding to the immobilized monomeric enzyme, but not crosslinker-stabilized oligomers. This suggests a preferential complex formation via homo-dimerization, rather than interactions with established oligomeric structures.
Schreiber
Daniela
D
Department of Biology, National University of Ireland, Maynooth, Co. Kildare, Ireland.
Ohlendieck
Kay
K
D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D017248:Enzyme Multiplied Immunoassay Technique; D008861:Microsomes / Q000737:chemistry; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000737:chemistry / Q000201:enzymology*; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism; D011817:Rabbits; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*
D009195:Peroxidase; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases