[Structural data on the myelin proteolipid of apparent molecular weight 20 kDa (DM-20)].
By a combination of chromatographic methods, we have obtained in an apparently homogeneous state the 24 kDa "major myelin proteolipid" (MMPL) and the 20 kDa "myelin proteolipid" (DM-20). Contrary to a commonly held view, the second one is not a conformationally different form of its major companion, as it differs markedly by its amino-acid composition, its electrophoretic behaviour after performic acid oxidation, and the results of tryptic digestion; however, they are obviously very closely related, as shown by the selective cleavages at the level of methionines and tryptophanes. These results are most simply interpreted by a single deletion in DM-20 of the hydrophilic fragment 100-140 of the (known) structure of the 24 kDa proteolipid. Lees' hypothesis of a deletion of fragment 197-267 cannot be retained.
D055598:Chemical Phenomena; D002621:Chemistry; D008970:Molecular Weight; D009185:Myelin Proteins; D011510:Proteolipids
D009185:Myelin Proteins; D011510:Proteolipids
Données structurales sur le protéolipide de la myéline de masse moléculaire apparente 20 kDa (DM-20).