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Studies on Malic Enzyme from Hymenolepis Diminuta

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.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc131474
Date12 1900
CreatorsLi, Tung
ContributorsHarris, Ben G., Gracy, Robert W.
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Format61 leaves : ill., Text
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Li, Tung

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