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dc.contributor.authorLou, Marjorie Jan-Yung Fengen_US
dc.date.accessioned2019-04-08T17:35:27Z
dc.date.issued1966
dc.date.submitted1966
dc.identifier.otherb14629859
dc.identifier.urihttps://hdl.handle.net/2144/34596
dc.descriptionThesis (Ph.D.)--Boston Universityen_US
dc.descriptionPLEASE NOTE: Boston University Libraries did not receive an Authorization To Manage form for this thesis or dissertation. It is therefore not openly accessible, though it may be available by request. If you are the author or principal advisor of this work and would like to request open access for it, please contact us at open-help@bu.edu. Thank you.en_US
dc.description.abstractIn Neurospora, as in other organisms, arginine and pyrimidine biosynthesis shares the common precursor, carbamyl phosphate. The fact that some mutants require only pyrimidines for growth while others require only arginine for growth indicates the possibility of two independent modes for carbamyl phosphate synthesis and utilization. The existence of two carbamyl phosphokinases has been hypothesized to resolve the interplay of nutritional requirements for arginine and pyrimidine. One carbamyl phosphokinase catalyzes the formation of carbamyl phosphate specific for the arginine pathway and the other carbamyl phosphokinase catalyzes the formation of carbamyl phosphate specific for the pyrimidine pathway [TRUNCATED]en_US
dc.language.isoen_US
dc.publisherBoston Universityen_US
dc.subjectArginineen_US
dc.subjectPyrimidineen_US
dc.subjectBiochemistryen_US
dc.titleInhibition of enzymes of the arginine and pyrimidine biosynthetic pathways by pyrimidine metabolitesen_US
dc.typeThesis/Dissertationen_US
dc.description.embargo2031-01-01
etd.degree.nameDoctor of Philosophyen_US
etd.degree.leveldoctoralen_US
etd.degree.disciplineBiochemistryen_US
etd.degree.grantorBoston Universityen_US
dc.identifier.barcode11719025638042
dc.identifier.mmsid99181148560001161


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