| pubmed-article:8280062 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0011602 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0313529 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8280062 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:8280062 | pubmed:dateCreated | 1994-2-7 | lld:pubmed |
| pubmed-article:8280062 | pubmed:abstractText | Dermatan sulphate (DS) obtained from bovine and pig mucosa and pig skin, and charge-enriched fractions of a selected DS preparation, were characterized in terms of charge density, M(r) and disaccharide composition of chondroitin ABC lyase digests, and by 13C-n.m.r. spectroscopy. Besides the major IdoA-GalNAc4SO3 sequences, all DS preparations contain about 10% disulphated disaccharide sequences (mostly IdoA2SO3-GalNAc4SO3, with minor amounts of IdoA-GalNAc4,6SO3). DS fragments (prepared by radical-catalysed depolymerization of DS and retaining the internal structure of the parent polysaccharide) as well as Smith degraded fragments [SD-DS, obtained by controlled degradation of periodate-oxidized and borohydride-reduced DS (RO-DS)] with the general structure GalNAc4SO3(IdoA2SO3-GalNAc4SO3)n-R (where R is the remnant of a glycol-split uronic acid, and n = 2-3 and 3-4) were characterized by one- and two-dimensional 1H-n.m.r., 13C-n.m.r. and disaccharide composition analysis. In accordance with previous findings [Maimone and Tollefsen (1990) J. Biol. Chem. 265, 18263-18271], only fragments with n > or = 3 significantly enhance the heparin cofactor II-mediated inhibition of thrombin. In natural DS preparations and their fractions, this activity (as well as the antithrombotic activity in an animal model) appears to require IdoA2SO3-containing sequences. The heparin cofactor II activity of DS, RO-DS and SD-DS fragments decreases with decreasing M(r). However, RO-DS fragments are more active than DS fragments of similar M(r), probably because of the extra flexibility endowed by glycol-split IdoA residues. | lld:pubmed |
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| pubmed-article:8280062 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8280062 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8280062 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8280062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8280062 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8280062 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8280062 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:TorriGG | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:GuerriniMM | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:MascellaniGG | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:CasuBB | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:BianchiniPP | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:ParmaBB | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:BisioAA | lld:pubmed |
| pubmed-article:8280062 | pubmed:author | pubmed-author:LiveraniLL | lld:pubmed |
| pubmed-article:8280062 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8280062 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8280062 | pubmed:volume | 296 ( Pt 3) | lld:pubmed |
| pubmed-article:8280062 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8280062 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8280062 | pubmed:pagination | 639-48 | lld:pubmed |
| pubmed-article:8280062 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8280062 | pubmed:meshHeading | pubmed-meshheading:8280062-... | lld:pubmed |
| pubmed-article:8280062 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8280062 | pubmed:articleTitle | Structure and contribution to the heparin cofactor II-mediated inhibition of thrombin of naturally oversulphated sequences of dermatan sulphate. | lld:pubmed |
| pubmed-article:8280062 | pubmed:affiliation | Opocrin S.p.A. Research and Development Laboratories, Corlo di Formigine, Modena, Italy. | lld:pubmed |
| pubmed-article:8280062 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8280062 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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