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
Interaction of calmodulin with chromatin associated proteins and myelin basic protien
โ Scribed by Yasushi Iwasa; Takafumi Iwasa; Kazuo Matsui; Kenji Higashi; Eishichi Miyamoto
- Book ID
- 118940712
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 458 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0024-3205
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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
The interaction of myelin basic protein with cholesterol and the conformational changes occurring in the protein upon interaction with the lipid were investigated. The myelin basic protein (MBP) plays an important role in stabilizing the multilamellar structure of the myelin membrane. MBP interacts