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Lymphocyte cell surface glycoproteins which bind to soybean and peanut lectins.
- Source :
- Immunology; Aug82, Vol. 46 Issue 4, p713-726, 14p
- Publication Year :
- 1982
-
Abstract
- In cellular immunology, peanut (Arachis hypogaea) lectin has been used to selectively agglutinate immature lymphoid cells and soybean (Glycine max) lectin to agglutinate B lymphocytes. We have used affinity chromatography to study the surface glycoproteins of rat and mouse lymphoid cells which bind to these lectins. Thymocyte and T and B lymphocyte glycoproteins were analysed either without modification (native) or after the removal of sialic acid with neuraminidase (asialo). The only native glycoprotein which was seen to bind to peanut lectin was the 95,000 mol. wt sialoglycoprorein from thymocytes. The equivalent molecule from T lymphocytes bound to peanut lectin only after neuraminidase digestion. Thus the selective agglutination of thymocytes by peanut lectin would seem to be due to a partial lack of sialic acid residues on the O-glycosidically-linked oligosaccharides of the thymocyte sialoglycoprotein. The B lymphocyte form of the leucocyte-common antigen was the only prominent native glycoprotein which was seen to bind to soybean lectin and this probably accounts for the specific binding of this lectin to B cells. The leucocyte-common antigens, in their asialo forms, from thymocytes and B and T lymphocytes differed in their binding to the lectins and this establishes that these glycoproteins which share antigenic determinants differ in their carbohydrate structures. [ABSTRACT FROM AUTHOR]
- Subjects :
- LYMPHOCYTES
GLYCOPROTEINS
CELL membranes
B cells
LECTINS
IMMUNOGLOBULINS
Subjects
Details
- Language :
- English
- ISSN :
- 00192805
- Volume :
- 46
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 13935026