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dc.contributor.advisorGrunclová, Lenka
dc.contributor.authorAbsolonová, Markéta
dc.date.accessioned2021-12-06T13:40:22Z
dc.date.available2021-12-06T13:40:22Z
dc.date.issued2011
dc.date.submitted2011-05-20
dc.identifier.urihttps://dspace.jcu.cz/handle/123456789/23783
dc.format22
dc.format22
dc.language.isoeng
dc.publisherJihočeská univerzitacze
dc.rightsBez omezení
dc.subjectIrAM4eng
dc.subject?2-macroglobulineng
dc.subjectIxodes ricinuseng
dc.subjectprotease inhibitoreng
dc.titleIrAM4: Partial characterisation of a molecule similar to \recke{alpha}<sub>2</sub>-macroglobulin from a tick <i>Ixodes ricinus</i>cze
dc.title.alternativeIrAM4: Partial characterisation of a molecule similar to \recke{alpha}<sub>2</sub>-macroglobulin from a tick <i>Ixodes ricinus</i>eng
dc.typebakalářská prácecze
dc.identifier.stag19686
dc.description.abstract-translatedIxodes ricinus is a hard tick that can transmit several diseases that are capable of affecting humans. Among those are tick-borne encephalitis and Lyme disease. The focus of this work is on IrAM4, a member of tick ?2-macroglobulin family (?2M-F) of proteins which belong to the evolutionarily oldest constituents of the innate immune system. ?2-macroglobulins are protease inhibitors and act primarily in inactivation of proteases secreted by invading pathogens within their infection cycle. The aim of this study was to identify ?2-M of Ixodes ricinus (IrAM4) from corresponding ortholog of protein ?2-M named IsAM4 present in the genome of closely related Ixodes scapularis. The partial sequence was determined by amplification of cDNA and subsequent sequencing of PCR products. RT-PCR tissue profiling revealed that IrAM4 is present in ovaries and salivary glands but not in the tick gut. The recombinant fragment of IrAM4 was afterwards prepared for immunization of a rabbit and the obtained polyclonal antibodies were used for Western blot analysis. The results showed that IrAM4 is mainly present in the hemolymph and probably in salivary glands and ovaries but it is not expressed in the gut. The native IrAM4 seems to be composed of two disulfide bound subunits. However, the exact structure of the molecule was not analyzed in this work.eng
dc.date.accepted2011-06-20
dc.description.departmentPřírodovědecká fakultacze
dc.thesis.degree-disciplineBiological Chemistrycze
dc.thesis.degree-grantorJihočeská univerzita. Přírodovědecká fakultacze
dc.thesis.degree-nameBc.
dc.thesis.degree-programBiochemistrycze
dc.description.gradeDokončená práce s úspěšnou obhajoboucze
dc.contributor.refereeUrbanová, Veronika


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