Abstract
The various isoforms of the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) are responsible for the Ca2+ uptake from the cytosol into the endoplasmic or sarcoplasmic reticulum (ER/SR). In some tissues, the activity of SERCA can be modulated by binding partners, such as phospholamban and sarcolipin. The activity of SERCA can be characterized by its apparent affinity for Ca2+ as well as maximal enzymatic velocity. Both parameters can be effectively determined by the protocol described here. Specifically, we describe the measurement of the rate of oxalate-facilitated 45Ca uptake into the SR of crude mouse ventricular homogenates. This protocol can easily be adapted for different tissues and animal models as well as cultured cells.
Original language | English (US) |
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Pages (from-to) | 161-170 |
Number of pages | 10 |
Journal | Methods in Molecular Biology |
Volume | 1377 |
DOIs | |
State | Published - 2016 |
Externally published | Yes |
Bibliographical note
Publisher Copyright:© Springer Science+Business Media New York 2016.
Keywords
- Ca
- Calcium affinity
- Calcium uptake
- K
- Oxalate
- Phospholamban
- SERCA
- Sarcolipin
- V