Malic enzyme from the rat tapeworm, Hymenolepis diminuta, has been purified 320-fold to a final specific activity of 29.4. The purification procedure included heat treatment, followed by column chromatography with Sephadex G-20, two phosphocellulose columns, and Sephadex G-200, respectively. The final purified enzyme appeared to be homogeneous on disc gel electrophoresis and G-200 gel filtration.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc131474 |
| Date | 12 1900 |
| Creators | Li, Tung |
| Contributors | Harris, Ben G., Gracy, Robert W. |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | 61 leaves : ill., Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Li, Tung |
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