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A Peanut Agglutinin Binding Glycoprotein in CNS Myelin and Oligodendrocytes
Author(s) -
MIKOL DANIEL D.,
SZUCHET SARA,
STEFANSSON KARI
Publication year - 1988
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1988.tb27118.x
Subject(s) - polyclonal antibodies , peanut agglutinin , myelin , myelin associated glycoprotein , glycoprotein , affinity chromatography , antibody , biochemistry , chemistry , microbiology and biotechnology , lectin , myelin oligodendrocyte glycoprotein , agglutinin , biology , central nervous system , immunology , endocrinology , enzyme
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.