BIOCHEMICAL AND IMMUNOHISTOCHEMICAL STUDIES WITH SPECIFIC POLYCLONAL ANTIBODIES DIRECTED AGAINST BOVINE MYELIN OLIGODENDROCYTE GLYCOPROTEIN

Bovine myelin/oligodendrocyte glycoprotein (MOG) was purified from a W olfgram protein fraction of brain myelin by molecular sieving and prep arative gel electrophoresis. The N-terminal sequence of this wheat ger m agglutinin reacting glycoprotein was determined. Antibodies against purified MOG and synthetic N-terminal octapeptide of MOG were produced in rabbits. Respective affinity purified antibody preparations gave i dentical results on Western blots. Treatment with specific glycosidase s indicated that the oligosaccharide chains of MOG are only of N-chain type. This glycoprotein seems to be restricted to mammalian species s ince it was not detected in other animal species, ranging from fish up to reptiles. Immunohistochemical investigations on rat brain sections revealed that MOG is restricted to myelin sheaths and oligodendrocyte s, thus corroborating previous results obtained with the MOG 8-18C5 mo noclonal antibody. Decreased staining pattern in Jimpy brain further a ttested its specific localization in myelin-related structures. The oc tapeptide site-specific antibodies were not reactive on brain sections which may be attributed to the burying of this N-terminal sequence in the membrane. These MOG polyclonal antibodies appear to be valuable t ools for further studies concerning this minor glycoprotein.