4.2 Article

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

期刊

GLYCOCONJUGATE JOURNAL
卷 19, 期 7-9, 页码 459-465

出版社

SPRINGER
DOI: 10.1023/B:GLYC.0000014075.62724.d0

关键词

galectin-1; galectin-3; galectin-7; thermodynamics; binding specificity

资金

  1. NCI NIH HHS [P30 CA-13330, CA-16054] Funding Source: Medline
  2. NATIONAL CANCER INSTITUTE [R01CA016054, P30CA013330] Funding Source: NIH RePORTER

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.2
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据