Literature DB >> 6370249

Organ specific alcohol metabolism: placental chi-ADH.

X Parés, J Farrés, B L Vallee.   

Abstract

Human placenta contains a single detectable isozyme of alcohol dehydrogenase that has been isolated and characterized. It migrates toward the anode on starch gel electrophoresis and can be stained with pentanol but not ethanol as substrate. Its kinetic and molecular characteristics are identical with those of the recently discovered chi-ADH (Class III) isozyme from human liver. Placental ADH is present in the cytosol of this organ in small amounts, 6 mg/kg fresh tissue. It oxidizes ethanol very slowly--even at ethanol concentrations that would reflect intoxication when found in serum. Thus, placental alcohol dehydrogenase cannot play a significant role in the ethanol metabolism of pregnant women.

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Year:  1984        PMID: 6370249     DOI: 10.1016/0006-291x(84)90880-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

Review 1.  Genome-wide association discoveries of alcohol dependence.

Authors:  Lingjun Zuo; Lingeng Lu; Yunlong Tan; Xinghua Pan; Yiqiang Cai; Xiaoping Wang; Jiang Hong; Chunlong Zhong; Fei Wang; Xiang-Yang Zhang; Lauren A Vanderlinden; Boris Tabakoff; Xingguang Luo
Journal:  Am J Addict       Date:  2014 Nov-Dec

2.  chi-ADH is the sole alcohol dehydrogenase isozyme of mammalian brains: implications and inferences.

Authors:  T B Beisswenger; B Holmquist; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1985-12       Impact factor: 11.205

3.  Aldehyde oxidation in human placenta. Purification and properties of 1-pyrroline-5-carboxylate dehydrogenase.

Authors:  J Farrés; P Julià; X Parés
Journal:  Biochem J       Date:  1988-12-01       Impact factor: 3.857

  3 in total

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