Quantitative aspects of the development of a hydrophobic binding site on calmodulin by calcium binding
β Scribed by Robert F. Steiner
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1984
- Tongue
- English
- Weight
- 614 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
The interactive binding by calmodulin of Ca2+ and 1-anilinonaphthalene-8-sulfonate (1,8-ANS) has been examined. In the presence of saturating levels of Ca2+, calmodulin develops one moderately strong binding site for 1,8-ANS, plus one or more weaker sites. The binding of 1,8-ANS by unliganded, or singly liganded, calmodulin is slight; the development of a strong binding site, as well as the characteristic fluorescence enhancement and CD spectrum, requires the binding of two Ca2+ ions. Little further change occurs on binding additional Ca2+ ions.
π SIMILAR VOLUMES
Calcium has been suggested as the second messenger link between skeletal muscle activity and AChR gene expression and synthesis. We have compared the concentrations of the Ca2+ channel antagonists D600 and nisoldipine needed both to block Ca2+ uptake into cultured myotubes and to increase AChR expre