Conformation and aggregation of bovine myelin proteins
β Scribed by Ronald E. Block; Al H. Brady; Seymour Joffe
- Book ID
- 118854354
- Publisher
- Elsevier Science
- Year
- 1973
- Tongue
- English
- Weight
- 356 KB
- Volume
- 54
- Category
- Article
- ISSN
- 0006-291X
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Controlled thrombic digestion of a preparation of components 2 + 3 isolated from the 18.5 kDa bovine myelin basic protein (MBP) yielded a polypeptide that was monophosphorylated on threonine 97 (component 3pT97). This is the first posttranslationally phosphorylated MBP isolated in pure
## Abstract The conformation of Ξ²βcasein A in the monomeric and thermally aggregated states has been investigated by a range of techniques. Ξ²βCasein exists as a monomer in solution at 4Β°C and at concentrations up to at least 3 g/dl. The molecule is flexible and exhibits a lot of segmental motion, b
Recent evidence suggests that myelin basic protein (MBP) exon-2-containing isoforms play a significant role in the onset of myelination because they are more abundant during early development. The pattern of expression of MBP exon-2-containing isoforms was studied in rat brain aggregate cultures dur