๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Interactions of free and immobilized myelin basic protein with anionic detergents

โœ 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

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Myelin basic protein: Interaction with c
โœ Dr. K.-F. J. Chan; N. D. Robb; W. H. Chen ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 849 KB

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 myelin basic protein and
โœ A. M. Edwards; N. W. Ross; J. B. Ulmer; P. E. Braun ๐Ÿ“‚ Article ๐Ÿ“… 1989 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 604 KB

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