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Expression of Binding Properties of Gal/GalNAc Reactive Lectins by Mammalian Glycotopes

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The Molecular Immunology of Complex Carbohydrates —2

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 491))

Abstract

Expression of the binding properties of Gal/GalNAc specific lectins, based on the affinity of decreasing order of mammalian glycotopes (determinants) rather than saccharide inhibition pattern, is probably one of the best ways to express hydrate specifity and should facilitate the selection of lectins as structural probes for ng mammalian glycobiology.

Eleven mammalian structural units have been selected to express the binding in of applied lectins. They are: 1. F, GalNAcαl→3GalNAc; 2. A, GalNAcαl→ 3Gal; 3. T, Galβ 1→ 3GalNAc; 4. I, Galβ 1→ 3GlcNAc; 5. II, Galβ1→4GlcNAc; 6. B, Galalα3Gal; 7. E, Galα1→4Gal; 8. L, Galβ1→4Glc; 9. P, GalNAcβ1→3Gal; 10. S, GalNAcβ1→4Gal and 11. Tn, GalNAcα1→Ser (Thr) of the de chain. Thus, the carbohydrate specificity of Gal/GalNAc reactive lectins can be ed into classes according to their highest affinity for the above disaccharides and/or sidue. Examples of the binding properties of these lectins can be demonstrated by us communis agglutinin (RCA1), grouped as II specific lectin and its binding rty is II > I > B > T; Abrus precatorills agglutinin (AP A), classified as T and its hydrate specificity is T > I/II > E > B > Tn; Artocarplls integrifolia Gacalin, AIL), as/T Tn specific and its binding reactivity is T > Tn > > I (II) and Geodia cydonillm), as F/A specific, and with affinity for F > Ah [ GalNAcαl→3(LFucα1→2)Gal] > >I>L.

Due to the multiple reactivity of lectins toward mammalian glycotopes, the ble existence of different combining sites or sub sites in the same molecule has to be ined, and the differential binding properties of these combining sites (if any) have to aracterized. To establish the relationship among the amino acid sequences of the ining sites of plant lectins and mammalian glycotopes should be an important ion to be addressed in lectinology.

Article FootNote

This paper is dedicaled to Dr. A. Herp, who has assisted my research for over two decades.

Article FootNote

This work was supported by Grants from Chang-Gung Medical Research Project (CMRP No. 676), Kwei-san, Tao-yuan, Taiwan and the National Science Counci I (NSC 87-2316-b-182-(05), Taipei, Taiwan.

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  1. Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, College of Medicine Chang-Gung University, Kwei-san, Tao yuan, 333, Taiwan

    Albert M. Wu

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  1. Glyco Research Laboratory Institutes of Basic Medical Sciences and Natural Products, College of Medicine Chang-Gung University, Kwei-san, Tay-yuan, Taiwan

    Albert M. Wu

  2. Tao-yuan, 333, Taiwan

    Albert M. Wu

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Wu, A.M. (2001). Expression of Binding Properties of Gal/GalNAc Reactive Lectins by Mammalian Glycotopes. In: Wu, A.M. (eds) The Molecular Immunology of Complex Carbohydrates —2. Advances in Experimental Medicine and Biology, vol 491. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1267-7_4

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