Chacko, BKAppukuttan, PS2012-12-042012-12-042001INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. 28; 5; 365-371http://dx.doi.org/10.1016/S0141-8130(01)00139-8https://dspace.sctimst.ac.in/handle/123456789/845Peanut (Arachis hypogaea) agglutinin (PNA) is extensively used as tumour marker as it strongly recognises the cancer specific T antigen (Ga1 beta --> 3GalNAc-), but not its sialylated version. However, an additional specificity towards Gal beta1 --> 4GlcNAc (LacNAc), which is not tumour specific, had been attributed to PNA. For correct interpretation of lectin histochemical results we examined PNA sugar specificity using naturally occurring or semi-synthetic glycoproteins, matrix-immobilised galactosides and lectin-binding tissue glycoproteins, rather than mono- or disaccharides as ligands. Dot-blots, transfer blots or polystyrene plate coatings of the soluble glycoconjugates were probed with horse-radish peroxidase (HRP) conjugates of PNA and other lectins of known specificity. Modifications of PNA-binding glycoproteins, including selective removal of O-linked oligosaccharides and treatment with glycosidases revealed that Gal beta1 --> 4GlcNAc (LacNAc) was ineffective while terminal alpha -linked galactose (TAG) as well as exposed T antigen (Gal beta1 --> 3 GalNAc-) was excellent as sugar moiety in glycoproteins for their recognition by PNA. When immobilised, melibiose was superior to lactose in PNA binding. Results were confirmed using TAG-specific human serum anti-a-galactoside antibody. (C) 2001 Elsevier Science B.V. All rights reserved.Biochemistry