Pyruvate carboxylase from Arthrobacter globiformis
Pyruvate carboxylase from Arthrobacter globiformis has been purified approximately 300-fold. The highly purified enzyme has a specific activity of 27.0 nmoles of oxaloacetate formed per mg of protein and gave two bands on SDS-polyacrylamide gel electrophoresis. The pyruvate caxboxylase containing ba...
| Main Author: | |
|---|---|
| Published: |
University of Leicester
1973
|
| Subjects: | |
| Online Access: | http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.674084 |