Abstract
Partially denatured main isoenzyme com- Key Words ponent of alcohol dehydrogenase from horse liver separates Denaturation of horse into three peaks on chromatography on Sephadex G-150, liver alcohol dehydrogenase with relative elution volume (Ve/Vo) values of 1.7,1.3 and in urea 1.0, respectively. The peak with Ve/Vo value of 1.7 consists of the native enzyme. The components of the peak with Ve/Vo value of 1.3 are able to form the native enzyme under suitable techniques and, therefore, may represent enzyme subunits, or possibly protein aggregates. The peak with Ve/Vo value of 1.0 probably represents subunit aggregates. The fact that reassociable forms of the enzyme are excluded by Sephadex G-150 in front of the native enzyme suggests that dissociation in urea is accompanied by considerable unfolding of the native structure. The denaturation rate is faster at 4 than at 20°C and aggregate formation is also faster at 4 then at 20°C. The rate of dénaturation of the enzyme, as determined by electrophoresis and scanning, is highly dependent on the purity of urea.
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