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Immunological and biochemical characterization of the human alcohol dehydrogenase χ‐ADH isozyme

Immunological and biochemical characterization of the human alcohol dehydrogenase χ‐ADH isozyme Summary 1. The recently identified χ‐ADH isozyme was purified from human liver and used to raise immune sera. 2. The χ 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. 3. χ‐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 β position. 4. We conclude that the locus, designated ADH5, encoding the χ isozyme has a separate evolutionary origin from the other ADH genes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annals of Human Genetics Wiley

Immunological and biochemical characterization of the human alcohol dehydrogenase χ‐ADH isozyme

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References (18)

Publisher
Wiley
Copyright
Copyright © 1984 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0003-4800
eISSN
1469-1809
DOI
10.1111/j.1469-1809.1984.tb00828.x
Publisher site
See Article on Publisher Site

Abstract

Summary 1. The recently identified χ‐ADH isozyme was purified from human liver and used to raise immune sera. 2. The χ 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. 3. χ‐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 β position. 4. We conclude that the locus, designated ADH5, encoding the χ isozyme has a separate evolutionary origin from the other ADH genes.

Journal

Annals of Human GeneticsWiley

Published: Jan 1, 1984

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