Abstract
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.
Degree
thesis:*- Name thesis:degree_name
- Ph. D.
- Level thesis:degree_level
- doctoral
- Discipline thesis:degree_discipline
- Biochemistry and Nutrition
- Department dc:contributor.department
- Biochemistry and Nutrition
- Grantor dc:publisher
- Virginia Tech
- Year dc:date.issued
- 1963
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Hegre, Carman Stanford
- Chair dc:contributor.committeechair
-
- Lane, M. Daniel
- Committee members dc:contributor.committeemember
-
- Engel, R. W.
- King, Kendall W.
- Cochran, Donald G.
- Moore, Walter E. C.
Rights
dc:rights- Statement dc:rights
-
- In Copyright
- Licence dc:rights.uri
- Language dc:language.iso
- en_US
Identifiers
dc:identifier.*- Dc Identifier Other
- etd-09082012-040230
- OAI identifier oai:identifier
- oai:vtechworks.lib.vt.edu:10919/39306