Studies of a hydrophobic myelin protein
Read Online

Studies of a hydrophobic myelin protein

  • 354 Want to read
  • ·
  • 51 Currently reading

Published by s.n.] in [Toronto? .
Written in English


  • Myelin,
  • Proteins

Book details:

Edition Notes

Statementby Jean Gagnon.
ContributionsToronto, Ont. University.
The Physical Object
Pagination[6], xvi, 214, [13] leaves, [2] leaves of plates :
Number of Pages214
ID Numbers
Open LibraryOL19470075M

Download Studies of a hydrophobic myelin protein


  A purified protein fraction from the proteolipids of human brain myelin was recombined with different lipids either in aqueous buffer or in a chloroformmethanol-water (10∶5∶1, v/v/v) mixture. It was found that under both conditions it binds strongly to phospholipids irrespective of surface charge, the presence of cholesterol or double bonds on the fatty acyl Cited by: CNS myelin is rich in myelin basic protein (MBP) and proteolipid protein (PLP). The major protein component of peripheral myelin (around 80%) is myelin protein zero (P0). This is a member of the immunoglobulin superfamily and is essential for compaction of adjacent myelin lamellae which enables axons to be tightly wrapped. Myelin is a lipid-rich (fatty) substance that surrounds nerve cell axons (the nervous system’s wires) to insulate them and increase the rate at which information (encoded as electrical impulses) is passed along the myelinated axon can be likened to an electrical wire (the axon) with insulating material (myelin) around it. However, unlike the plastic covering on an electrical wire FMA: The protein composition of myelin is relatively simple compared to that of other biological membranes, with a limited number of polypeptides constituting most of the myelin proteins. In both the central nervous system (CNS) and the peripheral nervous system (PNS), the major proteins are myelin-specific and are found only in myelin and myelin Cited by:

The effect which intrinsic (proteolipid) protein has on fluidity of central nervous system myelin membrane was measured through differences in temperature-dependent anisotropy of the lipid-soluble fluorescence probe, 1,6-diphenyl-1,3,5-hexatriene (DPH), in multilamellar vesicles (MLV) prepared from total myelin lipids in the presence and absence of proteolipid by: 3. The amino acid sequences of the encephalitogenic basic protein, A1, from bovine and human myelin are similar, differing by only 11 residues. The sequence reveals that while basic residues are spread randomly over most of the polypeptide chain, several regions ( residues) exist that are nonpolar in by: Synergistic interactions of lipids and myelin basic protein Article (PDF Available) in Proceedings of the National Academy of Sciences (37) October with Reads. N.m.r. studies of myelin basic protein. Conformation of a peptide that is an antigenic determinant for B-cell reactivity Article (PDF Available) in Biochemical Journal (2) August

Under these experimental conditions the kDa protein did not interact with the GTP-binding proteins. The fact that the myelin GTP-binding proteins in the active state formed complexes with a different set of proteins than when in the inactive state is a strong indication that these proteins are effector by: 4.   Myelin basic protein (MBP) is the second most abundant protein of central nervous system (CNS) myelin (after the proteolipid protein), representing about 30 % of the total myelin protein and about 10 % of myelin by weight. It is also present in peripheral nervous system (PNS) myelin but as a lower percentage of the total : Hardcover. Myelin basic protein (MBP) comprises about 20% of the myelin sheath in neuronal axons. MBP is commonly used to induce autoimmune encephalomyelitis in animal models. MBP is unique in its high degree of post-translational modifications including multiple phosphorylation sites, deamidation of glutamine and acetylation of alanine as well as. The myelin sheath is a greatly extended and modified plasma membrane, which is wrapped around the nerve axon in a spiral fashion. A comprehensive review of the older literature on the structure, biochemistry and other aspects of myelin is available in a book published 20 years ago [1], whereas newer developments in the myelin field are.