Lactate dehydrogenase was isolated in pure form from crude extract of the cestode Hymenoleois diminuta by heat treatment and column chromatography. The purified enzyme has a specific activity of 106 units per mg protein. The molecular weight of the purified protein was 75,000 as determined by Sephadex gel filtration and analytical ultracentrifugation. An equilibrium ultracentrifugation study suggests a subunit molecular weight of 39,000. From these data, a dimer form of the native enzyme is proposed.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc131460 |
| Date | 12 1900 |
| Creators | Burke, William F. |
| 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 | 55 leaves: ill., Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Burke, William F. |
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