Purification and Partial Structural and Functional Characterization of Mouse Myelin/Oligodendrocyte Glycoprotein

• DOI: 10.1111/j.1471-4159.1992.tb10040.x
• Publication Date: 2006-10-06T03:02:03Z
• Authors: Patrick Amiguet; Minnetta V. Gardi...; Jean‐Pierre Zanetta; Jean‐Marie Matthieu
• Keywords: Myelin-associated glycoprotein; Myelin oligodendrocyte glycoprotein

Abstract: The myelin/oligodendrocyte glycoprotein (MOG) is found exclusively in the CNS, where it localized on surface of myelin and oligodendrocyte cytoplasmic membranes. monoclonal antibody 8‐18C5 identifies MOG. Several studies have shown that anti‐MOG antibodies can induce demyelination, thus inferring an important role stability. In this study, we demonstrate MOG consists two polypeptides, with molecular masses 26 28 kDa. This doublet becomes a single 25‐kDa band after deglycosylation trifluoromethanesulfonic acid or peptide‐ N 4 ‐( ‐acetyl‐β‐glucosaminyl)asparagine amidase, indicating there are no few O‐linked sugars represents differential glycosylation. Partial trypsin cleavage, which also gave lower weight, confirmed idea. was purified by polyacrylamide gel electrophoresis, followed electroelution. Three N‐terminal sequences eight to amino acids were obtained. By western blot analysis, binding between cerebellar soluble lectin. does not seem belong signal‐transducing GTP‐binding proteins. Reduced concentrations observed jimpy quaking dysmyelinating mutant mice, giving further support its localization compact CNS.