Title page for ETD etd-09082012-040230


Type of Document Dissertation
Author Hegre, Carman Stanford
URN etd-09082012-040230
Title Studies on the mechanism of action of propionyl-CoA carboxylase
Degree PhD
Department Biochemistry and Nutrition
Advisory Committee
Advisor Name Title
Lane, M. Daniel Committee Chair
Cochran, D. G. Committee Member
Engel, R. W. Committee Member
King, Kendall W. Committee Member
Moore, W. E. C. Committee Member
Keywords
  • Enzymes
Date of Defense 1963-10-15
Availability restricted
Abstract
Propionyl-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 propionyl—CoA in the absence of ATP. Absolute stereospecificity was observed with regard to which a-hydrogen is replaced during the addition.
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