| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7789506 | Carbohydrate Polymers | 2015 | 9 Pages |
Abstract
Presently, an efficient protein tyrosine phosphatase 1B (PTP1B) inhibitor, named FYGL-n, was isolated from Ganoderma Lucidum and characterized for its structure and bioactivity. Structure and chain conformation of FYGL-n based on both chemical and spectroscopic analysis showed that FYGL-n was a hyperbranched heteropolysaccharide bonded with protein via both serine and threonine residues by O-type glycoside, and showed a sphere observed by AFM. Specifically, monosaccharide composition indicated that FYGL-n consisted of d-arabinose, d-galactose, l-rhamnose and d-glucose in a mole ratio of 0.08:0.21:0.24:0.47, with a molecular mass of 72.9Â kDa. The analysis of amino acids in FYGL-n indicated that there were 16 common amino acids, among which aspartic acid, glycine, serine, alanine, glutamic acid and threonine were the dominant components. Also it was demonstrated that FYGL-n could inhibit the PTP1B activity on a competitive mechanism in vitro.
Related Topics
Physical Sciences and Engineering
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Authors
Deng Pan, Linqiang Wang, Congheng Chen, Bingwen Hu, Ping Zhou,