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dc.contributor.authorKim Y.S.
dc.contributor.authorLinhardt, Robert J.
dc.date1989
dc.date.accessioned2022-06-27T17:15:44Z
dc.date.available2022-06-27T17:15:44Z
dc.date.issued1989-01-01
dc.identifier.citationStructural Features of Heparin and Their Effect on Heparin Cofactor II Mediated Inhibition of Thrombin, Y.S. Kim and R.J. Linhardt, Thrombosis Research, 53, 55-71 (1989).
dc.identifier.issn493848
dc.identifier.urihttps://doi.org/10.1016/0049-3848(89)90115-1
dc.identifier.urihttps://hdl.handle.net/20.500.13015/6012
dc.descriptionThrombosis Research, 53, 55-71
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractHeparins from different species and tissues show similar levels of ATIII and HCII mediated anti-IIa activities. On fractionation, chains containing predominantly ATIII or HCII activities could not be separated. Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin's ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. These results suggest that ATIII and HCII do not share a common binding site. Partial enzymatic depolymerization of heparin resulted in large oligosaccharides which could be purified and partially characterized. Although oligosaccharides of degree of polymerization (dp) 18 and 20 showed significant ATIII and HCII mediated anti-IIa activities no separation of these activities resulted. These data suggest however that a minimum chain length of dp18 was required for HCII mediated anti-IIa activity.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0049-3848(89)90115-1
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofThrombosis Research
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleStructural Features of Heparin and Their Effect on Heparin Cofactor II Mediated Inhibition of Thrombin
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0049-3848(89)90115-1
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dcterms.isVersionOfhttps://doi.org/10.1016/0049-3848(89)90115-1
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages55-71
rpi.description.volume53


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