Interactions of free and immobilized myelin basic protein with anionic detergents
โ Scribed by Burns, Peter F.; Campagnoni, Celia W.; Chaiken, Irwin M.; Campagnoni, Anthony T.
- Book ID
- 126859417
- Publisher
- American Chemical Society
- Year
- 1981
- Tongue
- English
- Weight
- 900 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-2960
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๐ SIMILAR VOLUMES
The structural characteristics of myelin basic protein (MBP) involved in protein-protein and protein-lipid interactions were investigated. Rabbit MBP could bind calmodulin (CaM) in the presence of Ca2+ to form a complex that remained undissociated in 8 M urea. However, no tight complex formation was
The interaction of myelin basic protein (MBP) and proteolipid protein (PLP) was studied using a microtitre well binding assay and the ligand-blot overlay technique. The binding of iodinated PLP to MBP that was immobilized on microtitre wells was saturable and reversible. Its selectivity was investig