Identification of peanut agglutinin-binding glycoproteins on immature human thymocytes.
Previous studies in our laboratory have shown that peanut agglutinin (PNA), a lectin specific for the disaccharide Gal beta 3GalNAc, binds to immature (cortical) thymocytes of mouse and man and not to the mature (medullary) cells. Using lectin overlay of protein blots and lectin-affinity chromatography, we have found that the major PNA-binding glycoproteins on total as well as on immature (PNA+) human thymocytes correspond to two bands of Mr 170,000 and 180,000. Another glycoprotein, of Mr 110,000, also binds PNA but to a lesser extent. All three glycoproteins contain sialic acid as demonstrated by cell surface labeling with NaIO4-NaB3H4, binding of wheat germ agglutinin, and reaction with alkaline phosphatase-hydrazide. After treatment with sialidase, binding of PNA to these glycoproteins is significantly enhanced.
D002846:Chromatography, Affinity; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D008970:Molecular Weight; D019158:N-Acetylneuraminic Acid; D019887:Peanut Agglutinin; D012794:Sialic Acids / Q000032:analysis; D013601:T-Lymphocytes / Q000032:analysis* / Q000145:classification
D006023:Glycoproteins; D037102:Lectins; D019887:Peanut Agglutinin; D012794:Sialic Acids; D019158:N-Acetylneuraminic Acid