Studies on the mechanism of action of propionyl-CoA carboxylase

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dc.contributor.authorHegre, Carman Stanforden
dc.contributor.committeechairLane, M. Danielen
dc.contributor.committeememberEngel, R. W.en
dc.contributor.committeememberKing, Kendall W.en
dc.contributor.committeememberCochran, Donald G.en
dc.contributor.committeememberMoore, Walter E. C.en
dc.contributor.departmentBiochemistry and Nutritionen
dc.date.accessioned2014-03-14T21:18:29Zen
dc.date.adate2012-09-08en
dc.date.available2014-03-14T21:18:29Zen
dc.date.issued1963-10-15en
dc.date.rdate2012-09-08en
dc.date.sdate2012-09-08en
dc.description.abstractPropionyl-CoA carboxylase has been purified to a state of near nomogeniety, and some of its enzymatic properties relating to substrate binding and mechanism of action have been studied. The enzyme was not found to catalyze the incorporation of solvent tritium at the c-carbon of propionylâ CoA in the absence of ATP. Absolute stereospecificity was observed with regard to which a-hydrogen is replaced during the addition.en
dc.description.degreePh. D.en
dc.format.extent74 leavesen
dc.format.mediumBTDen
dc.format.mimetypeapplication/pdfen
dc.identifier.otheretd-09082012-040230en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-09082012-040230/en
dc.identifier.urihttp://hdl.handle.net/10919/39306en
dc.language.isoen_USen
dc.publisherVirginia Techen
dc.relation.haspartLD5655.V856_1963.H437.pdfen
dc.relation.isformatofOCLC# 20269442en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subject.lccLD5655.V856 1963.H437en
dc.subject.lcshEnzymes -- Synthesisen
dc.titleStudies on the mechanism of action of propionyl-CoA carboxylaseen
dc.typeDissertationen
dc.type.dcmitypeTexten
thesis.degree.disciplineBiochemistry and Nutritionen
thesis.degree.grantorVirginia Polytechnic Instituteen
thesis.degree.leveldoctoralen
thesis.degree.namePh. D.en

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