Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/123224
Campo DC Valoridioma
dc.contributor.authorMoreno Indias,Isabelen_US
dc.contributor.authorA.W. Doddsen_US
dc.contributor.authorArgüello Henríquez, Anastasioen_US
dc.contributor.authorCastro Navarro, Noemíen_US
dc.contributor.authorR.B. Simen_US
dc.date.accessioned2023-06-05T09:02:57Z-
dc.date.available2023-06-05T09:02:57Z-
dc.date.issued2012en_US
dc.identifier.urihttp://hdl.handle.net/10553/123224-
dc.description.abstractComplement is a central component of the innate immune system which is involved in host defense against infectious agents. The complement system may be activated by three different pathways: the classical, the lectin and the alternative pathway. The complement system in mammals has been well described, and it is clear their complement systems are very similar, however, there are scanty research studies on goats. The aims of the present study were to contribute with new knowledge developing an efficient haemolytic assay for goats, affordable and easy to find worldwide; and to isolate the major complement system proteins from goat plasma, in order to raise antibodies to develop quantitative assays. The isolated proteins were C1q, the first protein involved in the classical pathway, factor H, because of its importance in the regulation of the alternative pathway, and C3, the most abundant protein which forms part of all three pathways. The main results were: 1) The commonly used sheep erythrocyte sensitized with rabbit antibodies were not sensitive to lysis by goat serum, but the combination of human RBC plus rabbit antibodies was the best option found for goat complement assay. A buffer based on HEPES instead of the classical veronal (barbitone) was developed. 2) Three proteins were isolated from gat serum: factor H, C1q and C3 and these were compared with the corresponding human proteins. A novel affinity chromatography technique was developed for isolation of factor H. In conclusion, human RBC plus rabbit antibodies were a suitable option for haemolytic assays, as well as the new buffer based on HEPES. The isolated proteins are similar to the human counterparts.en_US
dc.languageengen_US
dc.publisherInternational Goat Associationen_US
dc.source11th International Conference on Goatsen_US
dc.subject3104 Producción Animalen_US
dc.titleThe Complement System of the Goaten_US
dc.typeinfo:eu-repo/semantics/lectureen_US
dc.typeLectureen_US
dc.relation.conference11th International Conference on Goatsen_US
dc.description.lastpage60en_US
dc.description.firstpage60en_US
dc.investigacionCiencias de la Saluden_US
dc.type2Ponenciaen_US
dc.description.numberofpages1en_US
dc.utils.revisionen_US
dc.date.coverdateSeptiembre 2012en_US
dc.identifier.ulpgcen_US
dc.contributor.buulpgcBU-VETen_US
item.fulltextCon texto completo-
item.grantfulltextopen-
crisitem.author.deptGIR IUSA-ONEHEALTH 4. Producción y Biotecnología Animal-
crisitem.author.deptIU de Sanidad Animal y Seguridad Alimentaria-
crisitem.author.deptDepartamento de Patología Animal, Producción Animal, Bromatología y Tecnología de Los Alimentos-
crisitem.author.deptGIR IUSA-ONEHEALTH 4. Producción y Biotecnología Animal-
crisitem.author.deptIU de Sanidad Animal y Seguridad Alimentaria-
crisitem.author.deptDepartamento de Patología Animal, Producción Animal, Bromatología y Tecnología de Los Alimentos-
crisitem.author.orcid0000-0002-4426-0678-
crisitem.author.orcid0000-0002-3026-2031-
crisitem.author.parentorgIU de Sanidad Animal y Seguridad Alimentaria-
crisitem.author.parentorgIU de Sanidad Animal y Seguridad Alimentaria-
crisitem.author.fullNameMoreno Indias,Isabel-
crisitem.author.fullNameArgüello Henríquez, Anastasio-
crisitem.author.fullNameCastro Navarro, Noemí-
crisitem.event.eventsstartdate24-09-2012-
crisitem.event.eventsenddate27-09-2012-
Colección:Ponencias
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