A peanut agglutinin binding glycoprotein in CNS myelin and oligodendrocytes.
We isolated and characterized a 120-kd PNA-binding polypeptide from the human CNS. This polypeptide is linked to membranes through a PI linkage. After release from membranes by PLC it measures 105 kd, 30 kd of which appear to be contributed by N-linked carbohydrates. We isolated the polypeptide by the use of PLC and PNA affinity chromatography and used it to raise polyclonal antibodies and to determine the N-terminal sequence. Immunohistochemical and immunochemical studies using these antibodies showed that 120 kdpp is present in both myelin and oligodendrocytes.
Mikol
D D
DD
Department of Neurology, University of Chicago, Illinois 60637.
Szuchet
S
S
Stefansson
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002490:Central Nervous System / Q000032:analysis; D006801:Humans; D015151:Immunoblotting; D037102:Lectins / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009186:Myelin Sheath / Q000032:analysis*; D009457:Neuroglia / Q000032:analysis*; D009836:Oligodendroglia / Q000032:analysis*; D019887:Peanut Agglutinin; D010716:Phosphatidylinositols / Q000378:metabolism; D012756:Sheep; D010738:Type C Phospholipases / Q000378:metabolism
D037102:Lectins; D008562:Membrane Glycoproteins; D019887:Peanut Agglutinin; D010716:Phosphatidylinositols; D010738:Type C Phospholipases