Literature DB >> 6424546

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

A Adinolfi, M Adinolfi, D A Hopkinson.   

Abstract

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.

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Year:  1984        PMID: 6424546     DOI: 10.1111/j.1469-1809.1984.tb00828.x

Source DB:  PubMed          Journal:  Ann Hum Genet        ISSN: 0003-4800            Impact factor:   1.670


  5 in total

1.  Cross-reactive monoclonal antibodies to alcohol dehydrogenases.

Authors:  B G Talbot; G Bilodeau
Journal:  Experientia       Date:  1987-04-15

2.  Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase.

Authors:  R Kaiser; B Holmquist; B L Vallee; H Jörnvall
Journal:  J Protein Chem       Date:  1991-02

Review 3.  The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy.

Authors:  Scott D Barnett; Iain L O Buxton
Journal:  Crit Rev Biochem Mol Biol       Date:  2017-04-10       Impact factor: 8.250

4.  A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme.

Authors:  M Yasunami; C S Chen; A Yoshida
Journal:  Proc Natl Acad Sci U S A       Date:  1991-09-01       Impact factor: 11.205

5.  Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.

Authors:  T Ikuta; S Szeto; A Yoshida
Journal:  Proc Natl Acad Sci U S A       Date:  1986-02       Impact factor: 11.205

  5 in total

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