|Author||Chacko, B. K. ♦ Appukuttan, P. S.|
|Source||Sree Chitra Tirunal Institute for Medical Sciences & Technology|
|Publisher||International Journal of Biological Macromolecules|
|Subject Domain (in DDC)||Natural sciences & mathematics ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Technology ♦ Medicine & health|
|Subject Domain (in MeSH)||Carbohydrates ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Chemical Phenomena ♦ Biological Sciences|
|Abstract||Peanut (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.|
|Education Level||UG and PG|
|Learning Resource Type||Article|
|Educational Framework||Medical Council of India (MCI)|
|Journal||INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES|
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