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

被引:59
作者
Brewer, CF [1 ]
机构
[1] Albert Einstein Coll Med, Dept Mol Pharmacol & Microbiol & Immunol, Bronx, NY 10461 USA
关键词
galectin-1; galectin-3; galectin-7; thermodynamics; binding specificity;
D O I
10.1023/B:GLYC.0000014075.62724.d0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:459 / 465
页数:7
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