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IMMUNOLOGICAL PROPERTIES OF THE HUMAN ALCOHOL DEHYDROGENASE (ADH) ISOZYMES
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SUMMARYRabbit immune sera, raised against purified horse alcohol dehydrogenase (ADH) and against human β1β1 ADH isozyme, were found to react specifically against the enzyme. The antisera reacted against one or more common antigenic determinants of the ADH from primates and other mammals, indicating that common structures have been preserved in ADH over a long evolutionary period. The antisera did not react against Drosophila and yeast ADH.The human ADH isozymes coded by the three loci ADH1, ADH2 and ADH3, and the allelic variants, were immunologically indistinguishable. In contrast, the ‘anodal' form of human ADH showed no reaction with the immune sera, suggesting a separate evolutionary origin of this molecule. Results from the single radial diffusion test indicated that the high enzymatic activity of ‘atypical' human ADH was not associated with high concentrations of the enzyme protein.
Title: IMMUNOLOGICAL PROPERTIES OF THE HUMAN ALCOHOL DEHYDROGENASE (ADH) ISOZYMES
Description:
SUMMARYRabbit immune sera, raised against purified horse alcohol dehydrogenase (ADH) and against human β1β1 ADH isozyme, were found to react specifically against the enzyme.
The antisera reacted against one or more common antigenic determinants of the ADH from primates and other mammals, indicating that common structures have been preserved in ADH over a long evolutionary period.
The antisera did not react against Drosophila and yeast ADH.
The human ADH isozymes coded by the three loci ADH1, ADH2 and ADH3, and the allelic variants, were immunologically indistinguishable.
In contrast, the ‘anodal' form of human ADH showed no reaction with the immune sera, suggesting a separate evolutionary origin of this molecule.
Results from the single radial diffusion test indicated that the high enzymatic activity of ‘atypical' human ADH was not associated with high concentrations of the enzyme protein.
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