Methylmalonyl CoA mutase has been purified over 2300-fold from bovine brain using fractional precipitation, ion exchange resins, and gel filtration procedures. The crude extract had an equal mixture of mutase in the halo- and apoenzyme form. After the final purification step the ratio had changed to 86% holo-enzyme and 14% apoenzyme. The mutase enzyme had a pH optimum of 7. 0 in Tris-HCI buffer. The Km values for L-methylmalonyl CoA and succinyl CoA were 7.7 x 10^-4 M and 1.8 x 10^-4 M respectively. The equiIibrium constant in the direction of succinyl CoA formation was 19. Inhibition with N-ethylmalei-mide was noncompetitive with a K_i of 2.4 x 10^-3 M. The activity level of mutase in the brain was found to be about 5% of that found in liver.
| Identifer | oai:union.ndltd.org:BGMYU2/oai:scholarsarchive.byu.edu:etd-9305 |
| Date | 24 September 1974 |
| Creators | Martin, Damon |
| Publisher | BYU ScholarsArchive |
| Source Sets | Brigham Young University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
| Rights | http://lib.byu.edu/about/copyright/ |
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