Oligomerisation of Sarcoplasmic Reticulum Ca2+-ATPase Monomers from Skeletal Muscle

Daniela      Schreiber; Kay      Ohlendieck

doi:10.2174/092986607780090838

Abstract

The fast-twitch SERCA1 isoform of the sarcoplasmic reticulum Ca2+-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.

Keywords: Blot overlay, Ca2+-ATPase, Ca2+-uptake, oligomerisation, sarcoplasmic reticulum, SERCA

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Protein & Peptide Letters

Title: Oligomerisation of Sarcoplasmic Reticulum Ca2+-ATPase Monomers from Skeletal Muscle

Volume: 14 Issue: 3

Author(s): Daniela Schreiber and Kay Ohlendieck

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Keywords: Blot overlay, Ca2+-ATPase, Ca2+-uptake, oligomerisation, sarcoplasmic reticulum, SERCA

Abstract: The fast-twitch SERCA1 isoform of the sarcoplasmic reticulum Ca2+-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.

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Schreiber Daniela and Ohlendieck Kay, Oligomerisation of Sarcoplasmic Reticulum Ca2+-ATPase Monomers from Skeletal Muscle, Protein & Peptide Letters 2007; 14 (3) . https://dx.doi.org/10.2174/092986607780090838