Copper Uptake Induces Self-Assembly of 18.5 kDa Myelin Basic Protein (MBP)
نویسندگان
چکیده
منابع مشابه
Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoforms.
The classic myelin basic protein (MBP) splice isoforms range in nominal molecular mass from 14 to 21.5 kDa, and arise from the gene in the oligodendrocyte lineage (Golli) in maturing oligodendrocytes. The 18.5-kDa isoform that predominates in adult myelin adheres the cytosolic surfaces of oligodendrocyte membranes together, and forms a two-dimensional molecular sieve restricting protein diffusi...
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Aptamer ligands for myelin basic protein (MBP) were obtained using the systematic evolution of ligand by exponential enrichment (SELEX) method. Two clones were isolated from a pool of oligonucleotides and tested for MBP targeting. Using purified MBP, we demonstrated the binding activity of the aptamers and we also showed the affinity of MBP for oligonucleotides of specific length. Moreover, one...
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Myelin membranes prepared from rat brain possess both the enzyme and substrates to incorporate azP from (ya2P]ATP into membrane protein constituents. Qf the myelin polypeptides, only the two basic proteins were phosphorylated ; and both components appeared to be equally good substrates for endogenous or added protein kinases. The a2P was transferred primarily to serine residues of the basic pro...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2010
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.08.022