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
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
Affiliation:
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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Cite this article as:
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
DOI https://dx.doi.org/10.2174/092986607780090838 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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