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The Human Cell Surface Glycoprotein Complex (gp 120,200) Recognized by Monoclonal Antibody K20 is a Component Binding to Phytohaemagglutinin on T Cells
Author(s) -
AMIOT M.,
BERNARD A.,
TRAN H.C.,
LECA G.,
KANELLOPOULOS J. M.,
BOUMSELL L.
Publication year - 1986
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1986.tb01948.x
Subject(s) - glycoprotein , phytohaemagglutinin , monoclonal antibody , immunoprecipitation , microbiology and biotechnology , antibody , epitope , biology , cell , precipitin , lectin , biochemistry , immunology , in vitro
Monoclonal antibody K2H recognizes a human glycoprotein complex that is not rcstricted in haematopoietic lineages but is preferentially expressed on early haematopoietic cells, T cells, and monocytes This glycoprotein complex is made of constant ini 120,000–140,000 M 1 , subunitnoncovalently associated at the cell surface with subunits of higher M 1 . ranging from 150,000 to 200,000 on different cell types. Internal labelling with [ 35 S]methionine and pulse‐chase experiments revealed that in the cell the 120,000 M , glycoprotein of this complex is also noncnvalently associated with a 100,000 M t glycoprotein, and that both glycoproteins are independently biosynthesized. This glycoprotein complex is shown by immunoprecipitation by lectin plus antilectin antibodies and by sequential immunoprecipitation to be one one of the cell surface structures bound by phytohaemagglutinin on the surface of normal T cells.