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Identification of glycoproteins that are receptors for peanut agglutinin on immature (cortical) mouse thymocytes
Author(s) -
De Maio Antonio,
Lis Halina,
Gershoni Jonathan M.,
Sharon Nathan
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80045-x
Subject(s) - peanut agglutinin , glycoprotein , receptor , agglutinin , identification (biology) , biology , t cell receptor , microbiology and biotechnology , lectin , chemistry , immunology , biochemistry , t cell , immune system , botany
Binding of peanut agglutinin is being widely used as a marker for immature mouse thymocytes and for the separation of these cells from the mature thymocytes. Two cell surface glycoproteins that bind peanut agglutinin were detected on unfractionated as well as immature thymocytes by lectin overlay and affinity chromatography: one of M r between 170000 and 180000, and the other, a minor component, of M r 110000, both of which are partially sialylated. No receptors for peanut agglutinin were detected on the mature cells, whereas desialylation experiments revealed the presence of a glycoprotein of M r 110000. These findings were corroborated by electrophoretic analysis of cell surface glycoproteins of the isolated thymocyte subpopulations labeled in their carbohydrate moieties.