One molecular form of fumarase from Ascaris suum was demonstrated by cellulose acetate electroporesis and isoelectric focusing. The enzyme was partially purified by ammonium sulfate fractionation and ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified by ammonium sulfate fractionation amd ion-exchange chromatography to a specific activity of 49 units per mg protein. Enzymatic assay of the partially purified preparation showed glyceraldehyde-3-phosphate dehydrongenase to be the major preparative contaminant.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc798110 |
| Date | 05 1900 |
| Creators | Powley, David G. |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | 79 leaves : ill., Text |
| Rights | Public, Powley, David G., Copyright, Copyright is held by the author, unless otherwise noted. All rights |
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