Molecular and biochemical characterisation of variants of alpha-1-protease inhibitor isolated from asthmatic patients and synthesized by the process of site-directed mutagenesis

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dc.contributor.author Pillay, Visva
dc.date.accessioned 2018-02-13T10:01:28Z
dc.date.available 2018-02-13T10:01:28Z
dc.date.issued 2004-04-15
dc.identifier.uri https://hdl.handle.net/10539/23853
dc.description A dissertation submitted to the Faculty of Health Sciences, University of the Witwatersrand, Johannesburg, in fulfdment of the requirements for the degree of Doctor of Philosophy en_ZA
dc.description.abstract Asthma is a complex syndrome which has a significant inflammatory basis which results from the complex interactions between heterogenous genetic and environmental factors. Although the environmental allergens are fairly well known, little information concerning the genetic differences between atopic and non-atopic individuals is available. Alpha-1 antitrypsin is the archetypal member of the serine proteinase inhibitor or serpin superfamily and the most important proteinase inhibitor in the lung with specificity to neutrophil elastase. Genetic deficiency of the protein is classically associated with early onset emphysema, bronchiecstasis, panniculitis, rheumatoid arthritis and glomerulonephritis. The S(E264V), Z(E342K), Ml (213 Ala) and M2 (R101H) variants of alpha-1 antitrypsin have been implicated in the pathogenesis of asthma. A novel finding was the identification of 2 new variants, the M1E(JOhannesburg) and the M IN(johannesburg) associated with asthma in individuals from South Africa en_ZA
dc.language.iso en en_ZA
dc.subject.mesh Molecular Medicine
dc.subject.mesh Biochemical Phenomena
dc.subject.mesh Asthma
dc.subject.mesh Mutagenesis
dc.title Molecular and biochemical characterisation of variants of alpha-1-protease inhibitor isolated from asthmatic patients and synthesized by the process of site-directed mutagenesis en_ZA
dc.type Thesis en_ZA
dc.description.librarian IT2018 en_ZA


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