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dc.creatorRowe, Claire E.en_US
dc.date.accessioned2013-02-22T20:40:47Z
dc.date.available2013-02-22T20:40:47Z
dc.date.created2003en_US
dc.date.issued2013-02-22
dc.identifier.urihttp://hdl.handle.net/1969.1/ETD-TAMU-2003-Fellows-Thesis-R687en_US
dc.descriptionDue to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to digital@library.tamu.edu, referencing the URI of the item.en_US
dc.descriptionIncludes bibliographical references (leaf 21).en_US
dc.description.abstractOrganophosphorus hydrolase (OPH) is an enzyme capable of degrading toxic organophosphorus chemicals including the chemical warfare agents, sarin and VX, as well as many insecticides. This project seeks to understand how structure contributes to the enzyme's activity and stability by identifying regions of the enzyme necessary for each. PCR mutagenesis was used to create 67 variant forms of the gene that encodes OPH. Eight variant genes were then sequenced to locate the mutations in the enzymes' structure. Two of the eight variants contained only silent mutations and expressed wild-type OPH protein. The mutations made in two of the variants prevented the protein from being expressed. Characterization of the enzymes relative to two substrates, paraoxon and demeton-S, indicated that six variants had severely decreased activity. Five of these variants contained mutations in regions that have previously been shown to affect the enzyme's activity. Only one variant, 12, contained a mutation in a novel region of the enzyme.en_US
dc.format.mediumelectronicen_US
dc.format.mimetypeapplication/pdfen_US
dc.language.isoen_USen_US
dc.publisherTexas A&M Universityen_US
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries in 2008. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.en_US
dc.subjectgenetics.en_US
dc.subjectMajor genetics.en_US
dc.titleCharacterization of variant forms of organophosphorus hydrolaseen_US
thesis.degree.departmentgeneticsen_US
thesis.degree.disciplinegeneticsen_US
thesis.degree.nameFellows Thesisen_US
thesis.degree.levelUndergraduateen_US
dc.type.genrethesisen_US
dc.type.materialtexten_US
dc.format.digitalOriginreformatted digitalen_US


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