Immunological and biochemical characterization of the human alcohol dehydrogenase chi-ADH isozyme.

The recently identified chi-ADH isozyme was purified from human liver and used to raise immune sera. The chi form of ADH showed no structural resemblance to the ADH1, ADH2 and ADH3 (class I) or ADH4 (class II) isozymes, as judged by its immunological properties. chi-ADH was found in most human tissues including fetal specimens of 16 weeks gestational age and showed a preference for long chain primary alcohols with a double bond in the beta position. We conclude that the locus, designated ADH5, encoding the chi isozyme has a separate evolutionary origin from the other ADH genes.