Show simple item record

dc.contributor.authorLindhardt, Robert J.
dc.contributor.authorFitzgerald, Gerald L.
dc.contributor.authorCooney, Charles L.
dc.contributor.authorLanger, Robert
dc.date1982
dc.date.accessioned2022-06-27T17:16:06Z
dc.date.available2022-06-27T17:16:06Z
dc.date.issued1982-04-03
dc.identifier.citationMode of Action of Heparin Lyase On Heparin, R.J. Linhardt, G.L. Fitzgerald, C.L. Cooney, R. Langer, Biochimica et Biophysica Acta, 702, 197-203 (1982).
dc.identifier.issn1674838
dc.identifier.urihttps://doi.org/10.1016/0167-4838(82)90503-9
dc.identifier.urihttps://hdl.handle.net/20.500.13015/6040
dc.descriptionBiochimica et Biophysica Acta, 702, 197-203
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.abstractHeparinase (heparin lyase, EC 4.2.2.7) prepared from Flavobacterium heparinum was used to digest heparin. The products of digestion were examined with a viscosometric assay at various stages of the reaction to measure their average molecular weight. By comparison with computer simulations of various models, heparinase was shown to act in a random endolytic mode. The relative abundance of intermediates in heparin degradation catalyzed by heparinase immobilized on Sepharose 4B was measured by high pressure liquid chromatography (HPLC) at various time points. The results obtained using HPLC were consistent with a random endolytic mechanism. The heparin digestion products were separated and identified using gel permeation chromatography. The final distributions of heparin degradation products for free and immobilized heparinase were identical. Contaminating sulfatases and glycuronidases which could have subsequently acted on heparin degradation products were not found in significant amounts in the heparinase preparation studied.
dc.description.sponsorshipNational Institute of General Medical Sciences
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0167-4838(82)90503-9
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleMode of Action of Heparin Lyase On Heparin
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0167-4838(82)90503-9
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/0167-4838(82)90503-9
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.pages197-203
rpi.description.volume702


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record