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Volume :24 Issue : 2 1997      Add To Cart                                                                    Download

Structural characterization of a low molecular weight receptor for peanut agglutinin in murine lymphocytes

Auther : MOHAMED H. MANSOUR, FATMA ABDUL-SALAM AND MAGDA ADLY

 Department of Zoology, Faculty of Science, Kuwait University, P.O. Box 5969, Safat 13060, Kuwait

 ABSTRACT

A novel low molecular weight (LMW) receptor for the lectin peanut agglutinin (PNA) was characterized and purified from murine thymocytes and peripheral lymphocytes in the spleen. Preliminary binding assays with the fluoresceinated lectin demonstrated that the majority of I cortical thymocytes, and only a fraction of lymphocytes in the splenic white pulp, as well as other peripheral lymphoid organs were PNA-positive. This positivity was selectively inhibited by the preferred PNA disaccharide ligand (Gal/31,3GalNAc), indicating the specificity of the binding PNA receptors were purified from thymocytes and splenocytes by affinity chromatography on a PNA-agarose column, and their structural characteristics assessed by treatments with endoglycosidases and alkaline borohydride and analysis by two-dimensional (2-D) gels. Comparisons based on 2-D gels of glycosylated and deglycosylated forms were consistent with the thymic and splenic receptors, sharing a common 21 kDa polypeptide back- bone, which is subjected to differential post-translational N-linked glycosylations with one (thymic PNA receptor) or two and/or three (splenic PNA receptor) complex-type glycan units of distinct structures. Analyses of amino acid and carbohydrate compositions of the intact receptors confirmed these observations and revealed a comparatively high level of sialic acid residues in the splenic PNA receptor.

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