| dc.contributor | Universidade Estadual Paulista (UNESP) | |
| dc.creator | Watanabe, L. | |
| dc.creator | Vieira, D. F. | |
| dc.creator | Bortoleto, R. K. | |
| dc.creator | Arni, R. K. | |
| dc.date | 2014-05-20T14:02:18Z | |
| dc.date | 2014-05-20T14:02:18Z | |
| dc.date | 2002-06-01 | |
| dc.date.accessioned | 2017-04-05T21:27:07Z | |
| dc.date.available | 2017-04-05T21:27:07Z | |
| dc.identifier | Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 58, p. 1036-1038, 2002. | |
| dc.identifier | 0907-4449 | |
| dc.identifier | http://hdl.handle.net/11449/21953 | |
| dc.identifier | 10.1107/S0907444902003645 | |
| dc.identifier | WOS:000176271200017 | |
| dc.identifier | WOS000176271200017.pdf | |
| dc.identifier | http://dx.doi.org/10.1107/S0907444902003645 | |
| dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/867433 | |
| dc.description | Bothrombin, a snake-venom serine protease, specifically cleaves fibrinogen, releasing fibrinopeptide A to form non-crosslinked soft clots, aggregates platelets in the presence of exogeneous fibrinogen and activates blood coagulation factor VIII. Bothrombin shares high sequence homology with other snake-venom proteases such as batroxobin (94% identity), but only 30 and 34% identity with human alpha-thrombin and trypsin, respectively. Single crystals of bothrombin have been obtained and X-ray diffraction data have been collected at the Laboratorio Nacional de Luz Sincrotron to a resolution of 2.8 Angstrom. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 94.81, b = 115.68, c = 155.97 Angstrom. | |
| dc.language | eng | |
| dc.publisher | Blackwell Munksgaard | |
| dc.relation | Acta Crystallographica Section D: Biological Crystallography | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.title | Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca | |
| dc.type | Otro | |
