Interaction of myelin basic protein and proteolipid protein

@article{Edwards1989InteractionOM,
  title={Interaction of myelin basic protein and proteolipid protein},
  author={Anthony M. Edwards and N W Ross and Jeffrey B. Ulmer and Peter E. Braun},
  journal={Journal of Neuroscience Research},
  year={1989},
  volume={22}
}
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 investigated by the ligand‐blot overlay technique. Iodinated PLP was found to bind MBP but not any other CNS myelin proteins. This interaction was not dependent on the phosphoryl moiety of MBP. Binding of… 
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TLDR
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References

SHOWING 1-10 OF 18 REFERENCES
Structure of the Proteolipid Protein Extracted from Bovine Central Nervous System Myelin with Nondenaturing Detergents
TLDR
The proteolipid protein was isolated from Triton X‐100 extracts of myelin by adsorption onto phosphocellulose resin, with subsequent elution by 0.5 M sodium chloride was used as the final purification step.
Protein associations and basic protein conformation in the myelin membrane. The use of difluorodinitrobenzene as a cross-linking reagent.
TLDR
The near-neighbor relationships of proteins in the myelin membrane were examined using dinitrodifluorobenzene and other cross-linking reagents and found no evidence of intramolecular cross-links between the two peptides formed by N-bromosuccinimide cleavage or between theTwo peptide formed by cyanogen bromide Cleavage of the basic protein monomer.
Synthesis and incorporation of myelin polypeptides into CNS myelin
TLDR
It was found that crude myelin fractions are highly enriched in mRNAs coding for the MBPs but not in mRNA coding for PLP, which suggests that whereas the bound polysomes synthesizing PLP are largely confined to the cell body, free polysome synthesizing MBPs are concentrated in oligodendrocyte processes involved in myelination, which explains the immediate incorporation of MBPs into the developing myelin sheath.
Acylation in vitro of the myelin proteolipid protein and comparison with acylation in vivo: Acylation of a cysteine occurs nonenzymatically
TLDR
Comparison of proteolytically derived peptide maps showed that likely the same domain of PLP was acylated in vitro and in vivo.
Structural Organisation and Stability of Central Nervous System Myelin
TLDR
It is known that myelin, with its very high lipid to protein ratio, is at one end of a wide spectrum of biological membranes all of which appear to have a common structural organisation of complex lipids in a stable bilayer form in fluid-mosaic arrangement with proteins.
Diffraction Studies of Molecular Organization and Membrane Interactions in Myelin
TLDR
X-ray and neutron diffraction results on myelin can be correlated with its chemical composition, its structure as seen by electron microscopy (EM), and its responses to nerve conduction and to physical-chemical treatments, which has led to a description of the average distribution of lipid, protein, and water in the membrane array and to the localization of specific proteins and lipids within the myelin membrane bilayer.
Studies on Subcellular Fractions Which Are Involved in Myelin Assembly: Labeling of Myelin Proteins by a Double Radioisotope Approach Indicates Developmental Relationships
TLDR
Differences in ratio of the two leucine labels among proteins of myelin‐containing subfractions are interpreted as confirming metabolic differences relating to various stages of development rather than precursor‐product relationships.
The phosphorylation of myelin proteins
  • J. Ulmer
  • Biology, Chemistry
    Progress in Neurobiology
  • 1988
Molecular Organization of Myelin
TLDR
This chapter discusses in a critical way those studies from which the current concepts of myelin structure have evolved and to frame this discussion in the broader context of membrane structure that is emerging from other investigations.
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