Studies on human tonsillar lymphocyte membranes. II. Biological properties of membraneous glycoprotein fractions derived from human tonsillar lymphocytes.
Microsomal and mitochondrial glycoprotein fractions were isolated from human tonsillar lymphocytes. The microsomal glycoprotein was purified by DEAE-Sephadex chromatography. Yielding three subfractions. The different glycoprotein fractions were studied and characterized in two different ways. The isolated glycoproteins inhibited spontaneous (E) rosette formation. This effect was similar to that exhibited by some immunosuppressive drugs and the inhibitory property was heat-labile. The microsomal and mitochondrial glycoproteins and the DEAE-Sephadex subfractions of the microsomal glycoprotein inhibited the mitogenic effect of phytohaemagglutinin and concanavalin A. This inhibition was much stronger than the effect of monosaccharide haptens (N-acetyl-D-galactose-amine and D-glucose) and may be attributed to the lectin-binding property of the glycoprotein fraction.
D003208:Concanavalin A / Q000494:pharmacology; D006021:Glycophorins / Q000276:immunology; D006023:Glycoproteins / Q000276:immunology*; D006801:Humans; D066298:In Vitro Techniques; D037102:Lectins / Q000494:pharmacology; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000276:immunology*; D008565:Membrane Proteins / Q000276:immunology*; D008861:Microsomes / Q000276:immunology; D008928:Mitochondria / Q000276:immunology; D014066:Palatine Tonsil / Q000166:cytology*; D012397:Rosette Formation
D006021:Glycophorins; D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins; D003208:Concanavalin A