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Thermodynamic binding studies of galectin-1, -3 and -7

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Abstract

The carbohydrate binding specificities of the galectin family of animal lectins has been the source of intense recent investigations. Isothermal titration microcalorimetry (ITC) provides direct determination of the thermodynamics of binding of carbohydrates to lectins, and has provided important insights into the fine carbohydrate binding specificities of a wide number of plant and animal lectins. Recent ITC studies have been performed with galectin-1, galectin-3 and galectin-7 and their interactions with sialylated and non-sialylated carbohydrates. The results show important differences in the specificities of these three galectins toward poly-N-acetyllactosamine epitopes found on the surface of cells. Published in 2004.

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  1. Departments of Molecular Pharmacology, and Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, 10461, USA

    C. Fred Brewer

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  1. C. Fred Brewer
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Correspondence to C. Fred Brewer.

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Brewer, C.F. Thermodynamic binding studies of galectin-1, -3 and -7. Glycoconj J 19, 459–465 (2002). https://doi.org/10.1023/B:GLYC.0000014075.62724.d0

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  • DOI: https://doi.org/10.1023/B:GLYC.0000014075.62724.d0

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