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dc.contributor.authorGu., K.
dc.contributor.authorEdens, R.E.
dc.contributor.authorJandik, K.A.
dc.contributor.authorLinhardt, Robert J.
dc.date1993
dc.date.accessioned2022-06-27T17:14:38Z
dc.date.available2022-06-27T17:14:38Z
dc.date.issued1993
dc.identifier.citationMonoclonal Antibodies Prepared Against Heparin Lyase I and their Reactivity Towards Heparin Lyases I, II and III, K. Gu., R.E. Edens, K.A. Jandik, R.J. Linhardt, International Journal of Biochemistry, 25, 331-336 (1993).
dc.identifier.urihttps://doi.org/10.1016/0020-711X(93)90621-K
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5980
dc.descriptionInternational Journal of Biochemistry, 25, 331-336
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.abstract1. Six different monoclonal IgG mouse antibodies to heparin lyase I from Flavobacterium heparinum were prepared. 2. The monoclonal antibodies were used to detect heparin lyases I, II and III by dot-blotting immunoassay and by Western blotting. 3. Individual antibodies showed different reactivity toward the three heparin lyases. 4. The reactivity of two of the monoclonal antibodies was destroyed by exposing heparin lyases to sodium dodecyl sulfate. 5. The antibodies can be used to rapidly distinguish between the three heparin lyases.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0020-711X(93)90621-K
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleMonoclonal Antibodies Prepared Against Heparin Lyase I and their Reactivity Towards Heparin Lyases I, II and III
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0020-711X(93)90621-K
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)


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