Developmental Regulation of Pyrimidine Biosynthesis in Dictyostelium discoideum

dc.contributor.advisor	Wild, James R.
dc.creator	Jones, Brenda L.
dc.date.accessioned	2022-04-04T13:38:35Z
dc.date.available	2022-04-04T13:38:35Z
dc.date.issued	1982
dc.identifier.uri	https://hdl.handle.net/1969.1/CAPSTONE-WillardR_1998
dc.description	Program year: 1981/1982	en
dc.description	Digitized from print original stored in HDR	en
dc.description.abstract	The research reported in this thesis demonstrates that the initial steps for pyrimidine biosynthesis in the cellular slime mold Dictyostelium discoideum are catalyzed by the enzymes carbamoyl phosphate synthetase (CPSase, EC 2.7.2.9) and aspartate transcarbamoylase (ATCase, EC 2.1.3.1). Furthermore, it has been observed that the crude cell-free extract from Oictyostelium discoideum possesses a non-dialyzable inhibitory component of CPSase. It was striking to note that this inhibitory component interfered with CPSase activity from Escherichia coli as well.	en
dc.format.extent	24 pages	en
dc.format.medium	electronic	en
dc.format.mimetype	application/pdf
dc.subject	Dictyostelium discoideum	en
dc.subject	cellular slime mold	en
dc.subject	carbamoyl phosphate synthetase	en
dc.subject	CPSase	en
dc.subject	aspartate transcarbamoylase	en
dc.subject	ATCase	en
dc.subject	non-dialyzable inhibitory component	en
dc.title	Developmental Regulation of Pyrimidine Biosynthesis in Dictyostelium discoideum	en
dc.type	Thesis	en
thesis.degree.department	Biology	en
thesis.degree.grantor	University Undergraduate Fellow	en
thesis.degree.level	Undergraduate	en
dc.type.material	text	en