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Purification and Studies of Methylglyoxal Reductase from Sheep Liver

The objectives of these investigations were (1) the purification of MG reductase from sheep liver and (2) studies of some of its characteristics. MG reductase was purified 40 fold and showed a single band on SDS-PAGE. Molecular weight estimations with SDS-PAGE showed a molecular weight of 44,000; although gel filtration with Sephadex G-150 gave a molecular weight of 87,000 indicating that the enzyme might be a dimer. The Km for MG is 1.42 mM and for NADH it is 0.04 mM. The pH optimum for the purified enzyme is pH 7.0. Isoelectric focusing experiments showed a pI of 9.3. In vivo experiments involving rats treated with 3,3',5-triiodothyronine (T_3) and 6-n-propyl-2-thiouracil (PTU) indicated that MG reductase was depressed by T_3 and elevated by PTU.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc504292
Date05 1900
CreatorsLambert, Patricia A.
ContributorsNorton, S. J., Masaracchia, Ruthann A., Thompson, Richard E.
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatv, 44 leaves : ill., Text
RightsPublic, Lambert, Patricia A., Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved.

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