Interaction between Ca2+ and dipalmitoylphosphatidylcholine membranes: II. Fluorescence anisotropy study
โ Scribed by Ryoichi Kataoka; Shuji Aruga; Shigeki Mitaku; Kazuhiko Kinosita Jr.; Akira Ikegami
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 582 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0301-4622
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Abstract Human red blood cells (RBC) contain a cytoplasmic, nonhemoglobin protein which activates the (Ca^2+^โMg^2+^) ATPase of isolated RBC membranes. Results presented in this paper confirm that activation of (Ca^2+^โMg^2+^)ATPase is associated with binding of the cytoplasmic activator to the
Chloroplast proteins were phosphorylated under two test conditions: 'white light' irradiance alone and 'white light' irradiance with the addition of glucose and glucose oxidase, used to produce an anaerobic medium. The interaction of phospho-LHC II with Photosystem 1 (PS 1) was studied for two types
The interaction of dipalmitoylphosphatidylglycerol (DPPG) liposomes with divalent ions of magnesium, calcium and barium has been investigated with laser-Raman spectroscopy over the temperature range of 0-60ยฐC. The effect of Ca 2+ ions was also investigated as a function of concentration. At a Ca2+/D