Source:http://linkedlifedata.com/resource/pubmed/id/10569284
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-12-17
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pubmed:abstractText |
Glycosaminoglycans including dermatan sulphate, hyaluronan, heparan sulphate and heparin were chemically modified by O-sulphonation. By altering the reaction conditions, products having a different degree of O-sulphonation could be obtained. Glycosaminoglycan derivatives were prepared having no free hydroxyl groups, with sulphoester group/disaccharide unit ratios of 4.0 for dermatan sulphate and hyaluronan, and sulphoester and sulphamide group/disaccharide unit ratios of 4.22 and 4.88 for heparan sulphate and heparin, respectively. 1H NMR spectroscopy showed that the fully O-sulphonated hyaluronan derivative had a glucuronate residue with an altered conformation. Since glycosaminiglycans and their derivatives are often used as anticoagulant/antithrombotic agents, their anti-amidolytic activities were determined. The anti-factor IIa activity of fully O-sulphonated dermatan sulphate, hyaluronan and heparan sulphate ranged from 40 to 80 units/mg, while no anti-factor Xa activity of the fully O-sulphonated glycosaminoglycans was detected. These values are lower than those reported for low-molecular-weight heparins and are consistent with the requirement of an antithrombin III pentasaccharide binding site for anti-factor Xa activity. Interestingly, the anti-factor Xa of heparin is lost by chemical O-sulphonation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticoagulants,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Factor IIa,
http://linkedlifedata.com/resource/pubmed/chemical/Factor Xa,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Prothrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Uronic Acids
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0141-8130
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
233-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10569284-Anticoagulants,
pubmed-meshheading:10569284-Blood,
pubmed-meshheading:10569284-Disaccharides,
pubmed-meshheading:10569284-Factor Xa,
pubmed-meshheading:10569284-Glycosaminoglycans,
pubmed-meshheading:10569284-Humans,
pubmed-meshheading:10569284-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10569284-Molecular Weight,
pubmed-meshheading:10569284-Prothrombin,
pubmed-meshheading:10569284-Spectrophotometry, Infrared,
pubmed-meshheading:10569284-Structure-Activity Relationship,
pubmed-meshheading:10569284-Uronic Acids
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pubmed:year |
1999
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pubmed:articleTitle |
Preparation and anticoagulant activity of fully O-sulphonated glycosaminoglycans.
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pubmed:affiliation |
Faculty of Pharmaceutical Sciences, Chiba University, Inage, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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