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A Less Toxic Heparin Antagonist—Low Molecular Weight Protamine
dc.contributor.authorLiang, Jun Fengen_US
dc.contributor.authorZhen, L.en_US
dc.contributor.authorChang, Li-Chienen_US
dc.contributor.authorYang, Victor C.en_US
dc.date.accessioned2006-09-11T16:28:32Z
dc.date.available2006-09-11T16:28:32Z
dc.date.issued2003-01en_US
dc.identifier.citationLiang, J. F.; Zhen, L.; Chang, L.-C.; Yang, V. C.; (2003). "A Less Toxic Heparin Antagonist—Low Molecular Weight Protamine." Biochemistry (Moscow) 68(1): 116-120. <http://hdl.handle.net/2027.42/45793>en_US
dc.identifier.issn0006-2979en_US
dc.identifier.issn1608-3040en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/45793
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=12693985&dopt=citationen_US
dc.description.abstractA new thirteen amino acid peptide, named low molecular weight protamine (LMWP), was obtained through the enzymatic digestion of native protamine. Both in vitro and in vivo results showed that LMWP fully maintained the heparin neutralization function of protamine but had much lower immunogenicity and antigenicity. Unlike protamine, neither LMWP nor LMWP/heparin complexes caused significant blood platelet aggregation in rats. These results suggest that LMWP can be used as a substitute for protamine for developing a new generation of nontoxic heparin antagonists.en_US
dc.format.extent77512 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers-Plenum Publishers; MAIK “Nauka/Interperiodica” ; Springer Science+Business Mediaen_US
dc.subject.otherPlatelet Aggregationen_US
dc.subject.otherBiochemistry, Generalen_US
dc.subject.otherLife Sciencesen_US
dc.subject.otherLow Molecular Weight Protamineen_US
dc.subject.otherImmunogenicityen_US
dc.subject.otherHeparin Neutralizationen_US
dc.titleA Less Toxic Heparin Antagonist—Low Molecular Weight Protamineen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumCollege of Pharmacy, The University of Michigan, 428 Church str., Ann Arbor, MI, 48109-1065, USAen_US
dc.contributor.affiliationumCollege of Pharmacy, The University of Michigan, 428 Church str., Ann Arbor, MI, 48109-1065, USAen_US
dc.contributor.affiliationumCollege of Pharmacy, The University of Michigan, 428 Church str., Ann Arbor, MI, 48109-1065, USAen_US
dc.contributor.affiliationumCollege of Pharmacy, The University of Michigan, 428 Church str., Ann Arbor, MI, 48109-1065, USAen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid12693985en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/45793/1/10541_2004_Article_462566.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1023/A:1022109905487en_US
dc.identifier.sourceBiochemistryen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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