期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1721, 期 1-3, 页码 1-8出版社
ELSEVIER
DOI: 10.1016/j.bbagen.2004.09.007
关键词
heparan sulfate; human liver; structure; glycosaminoglycan; proteoglycan
资金
- NHLBI NIH HHS [R01 HL062244-05A1] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038060, R01 GM038060-19] Funding Source: Medline
The isolation, purification and structural characterization of human liver heparan sulfate are described. H-1-NMR spectroscopy demonstrates the purity of this glycosaminoglycan (GAG) and two-dimensional H-1-NMR confirmed that it was heparan sulfate. Enzymatic depolymerization of the isolated heparan sulfate, followed by gradient polyacrylamide gel, confirmed its heparin lyase sensitivity. The concentration of resulting unsaturated disaccharides was determined using reverse phase ion-pairing (RPIP) HPLC with post column derivatization and fluorescence detection. The results of this analysis clearly demonstrate that the isolated GAG was heparan sulfate, not heparin. Human liver heparan sulfate was similar to heparin in that it has a reduced content of unsulfated disaccharide and an elevated average sulfation level. The antithrombin-mediated anti-factor Xa activity of human liver heparan sulfate, however, was much lower than porcine intestinal (pharmaceutical) heparin but was comparable to standard porcine intestinal heparan sulfate. Moreover, human liver heparan sulfate shows higher degree of sulfation than heparan sulfate isolated from porcine liver or from the human hepatoma Hep 2G cell line. (C) 2004 Elsevier B.V. All rights reserved.
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