Purification and characterization of platelet aggregation inhibitors from snake venoms
dc.contributor.author | Trikha, Mohit | en_US |
dc.contributor.author | Rote, William E. | en_US |
dc.contributor.author | Manley, Peter J. | en_US |
dc.contributor.author | Lucchesi, Benedict Robert | en_US |
dc.contributor.author | Markland, Francis S. | en_US |
dc.date.accessioned | 2006-04-10T18:25:26Z | |
dc.date.available | 2006-04-10T18:25:26Z | |
dc.date.issued | 1994-01-01 | en_US |
dc.identifier.citation | Trikha, Mohit, Rote, William E., Manley, Peter J., Lucchesi, Benedict R., Markland, Francis S. (1994/01/01)."Purification and characterization of platelet aggregation inhibitors from snake venoms." Thrombosis Research 73(1): 39-52. <http://hdl.handle.net/2027.42/31863> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1C-4C4FHX7-5/2/7876cb3a0592affd4fff66c85d27e22a | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31863 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8178312&dopt=citation | en_US |
dc.description.abstract | Proteins that inhibit glycoprotein (GP) IIb/IIIa mediated platelet aggregation have been purified from the venom of two snake species. A small platelet aggregation inhibitor (pl.AI), multisquamatin (Mr=5,700), was purified from Echis multisquamatus venom by hydrophobic interaction HPLC and two steps on C18 reverse phase HPLC. A larger pl.AI, contortrostatin (Mr=15,000), was purified by a similar HPLC procedure from the venom of Agkistrodon contortrix contortrix. Both pl.AIs inhibit ADP-induced human, canine and rabbit platelet aggregation using platelet rich plasma (PRP). Multisquamatin has an IC50 of 97 nM, 281 nM and 333 nM for human, canine and rabbit PRP, respectively. Contortrostatin has an IC50 of 49 nM, 120 nM and 1,150 nM for human, canine and rabbit PRP, respectively. In a competitive binding assay using 125I-7E3 (a monoclonal antibody to GPIIb/IIIa that inhibits platelet aggregation) both contortrostatin and multisquamatin demonstrated GPIIb/IIIa specific binding to human and canine platelets. The IC50 for contortrostatin displacement of 7E3 binding to human and canine GPIIb/IIIa is 27 nM and 16 nM, respectively and for multisquamatin it is 3 nM and 63 nM, respectively. Our results indicate that both pl.AIs inhibit platelet aggregation by binding with high affinity to GPIIb/IIIa. | en_US |
dc.format.extent | 1087193 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Purification and characterization of platelet aggregation inhibitors from snake venoms | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Internal Medicine and Specialties | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Department of Biochemistry and Molecular Biology, University of Southern California, School of Medicine, Los Angeles, CA, USA | en_US |
dc.contributor.affiliationother | Department of Biochemistry and Molecular Biology, University of Southern California, School of Medicine, Los Angeles, CA, USA | en_US |
dc.identifier.pmid | 8178312 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31863/1/0000813.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0049-3848(94)90052-3 | en_US |
dc.identifier.source | Thrombosis Research | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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