Ryanodine as a functional probe of the skeletal muscle sarcoplasmic reticulum Ca2+release channel
โ Scribed by Gerhard Meissner; Anita El-Hashem
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 336 KB
- Volume
- 114
- Category
- Article
- ISSN
- 0300-8177
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โฆ Synopsis
Ryanodine is a neutral plant alkaloid which functions as a probe for an intracellular Ca2+ release channel (ryanodine receptor) in excitable tissues. Using [3H]ryanodine, a 30 S protein complex comprised of four polypeptides of Mr 565,000 has been isolated and functionally reconstituted into planar lipid bilayers. The effects of salt concentration and divalent cations on skeletal muscle sarcoplasmic reticulum [3H]ryanodine binding and Ca2+ release channel activity have been compared. These studies suggest that ryanodine is a good probe for investigating the function of the release channel.
๐ SIMILAR VOLUMES
Rapid mixing-vesicle ion flux and planar lipid bilayer-single channel measurements have shown that a high-conductance, ligand-gated Ca2+ release channel is present in 'heavy', junctional-derived membrane fractions of skeletal and cardiac muscle sarcoplasmic reticulum. Using the release channel-speci
Annexin VI has eight highly conserved repeated domains; all other annexins have four. Diaz-Muiioz et al. ( J Biol Chem 265:15894, 1990) reported that annexin VI alters the gating properties of the ryanodine-sensitive Ca2+-release channel isolated from sarcoplasmic reticulum. To investigate the domai