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dc.contributor.advisorButler, O. D.
dc.creatorKettner, Charles Adrian
dc.description.abstractA number of methyl ketones have been prepared from L-leucine and found to be competitive inhibitors of Aeromonas aminopeptidase. These inhibitors were leucine methyl ketone (K[subscript i] 18 μM), leucine chloromethyl ketone (k[subscript i] 0.67 μM), and leucine bromomethyl ketone (K[subscript i] 0.20 μM), and the corresponding succinimido derivative (K[subscript i] 170 μM), succinamic acid derivative (K[subscript i] 6.9 μM), and phthalimido derivative (K[subscript i] 140 μM). Reversible inhibition was observed for all of the inhibitors tested, indicating that the active site of this enzyme is not alkylated or acylated by the nucleophile-sensitive components of some of the inhibitors. One of the above inhibitors, the succinamic acid derivative of leucine bromomethyl ketone, was successfully used a ligand in affinity chromatography. The blocked form of this inhibitor was coupled to aminomethyl cellulose and then deblocked in aqueous trifluoroacetic to yield and insolubilized analog of an NH₂-terminal L-leucine residue. ...en
dc.format.extent67 leavesen
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries. 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
dc.subject.classification1974 Dissertation K44
dc.titleA bio-organic approach to the study of Aeromonas aminopeptidaseen
dc.typeThesisen A&M Universityen of Philosophyen
dc.contributor.committeeMemberCamp, B. J.
dc.contributor.committeeMemberCooper, R. J.
dc.contributor.committeeMemberDill, C. W.
dc.contributor.committeeMemberKing, G. T.
dc.contributor.committeeMemberRiggs, J. K.
dc.format.digitalOriginreformatted digitalen
dc.publisher.digitalTexas A&M University. Libraries

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