| 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 |
|
| 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.
|
| Files |
| Filename |
Size |
Approximate Download Time
(Hours:Minutes:Seconds)
|
| 28.8 Modem |
56K Modem |
ISDN (64 Kb) |
ISDN (128 Kb) |
Higher-speed Access |
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LD5655.V856_1963.H437.pdf |
3.26 Mb |
00:15:06 |
00:07:46 |
00:06:48 |
00:03:24 |
00:00:17 |
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