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IMMUNOLOGICAL PROPERTIES OF THE HUMAN ALCOHOL DEHYDROGENASE (ADH) ISOZYMES
Author(s) -
Adinolfi A.,
Adinolfi M.,
Hopkinson D. A.,
Harris H.
Publication year - 1978
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1978.tb00657.x
Subject(s) - isozyme , alcohol dehydrogenase , antiserum , enzyme , biology , biochemistry , allele , antigen , microbiology and biotechnology , genetics , gene
SUMMARY Rabbit immune sera, raised against purified horse alcohol dehydrogenase (ADH) and against human β 1 β 1 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 ADH 1 , ADH 2 and ADH 3 , 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.