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

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

The carbohydrate binding specificities of the galectin family of animal lectins has been the source of intense recent Investigations. Isothermal titration mlcrocalorlmetry (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.

Original languageEnglish (US)
Pages (from-to)459-465
Number of pages7
JournalGlycoconjugate Journal
Volume19
Issue number7-9
DOIs
StatePublished - 2002

Fingerprint

Galectin 1
Galectin 3
Galectins
Thermodynamics
Carbohydrates
Lectins
Titration
Plant Lectins
Epitopes

Keywords

  • Binding specificity
  • Galectin-1
  • Galectin-3
  • Galectin-7
  • Thermodynamics

ASJC Scopus subject areas

  • Biochemistry

Cite this

Thermodynamic binding studies of galectin-1, -3 and -7. / Brewer, Curtis F.

In: Glycoconjugate Journal, Vol. 19, No. 7-9, 2002, p. 459-465.

Research output: Contribution to journalArticle

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