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人类乙醇脱氢酶chi-ADH同工酶的免疫学和生物化学特性

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

作者信息

Adinolfi A, Adinolfi M, Hopkinson D A

出版信息

Ann Hum Genet. 1984 Jan;48(1):1-10. doi: 10.1111/j.1469-1809.1984.tb00828.x.

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

摘要

最近鉴定出的chi-ADH同工酶是从人肝脏中纯化出来的,并用于制备免疫血清。根据其免疫特性判断,ADH的chi形式与ADH1、ADH2和ADH3(I类)或ADH4(II类)同工酶没有结构相似性。在包括孕16周胎儿标本在内的大多数人体组织中都发现了chi-ADH,并且它对β位带有双键的长链伯醇具有偏好性。我们得出结论,编码chi同工酶的基因座(命名为ADH5)与其他ADH基因有独立的进化起源。

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