PMID: 3756202Oct 3, 1986Paper

Purification of aldehyde dehydrogenase reconstitutively active in fatty alcohol oxidation from rabbit intestinal microsomes

Biochimica Et Biophysica Acta
K IchiharaM Kusunose

Abstract

This work presents the purification and further characterization of the aldehyde dehydrogenase reconstitutively active in fatty alcohol oxidation, from rabbit intestinal microsomes. Microsomal aldehyde dehydrogenase was solubilized with cholate and purified by using chromatography on 6-amino-n-hexyl-Sepharose and 5'-AMP-Sepharose. The purified enzyme migrated as a single polypeptide band with molecular weight of 60,000 on SDS-polyacrylamide gel. By gel filtration in the presence of detergent, its apparent molecular weight was estimated to be 370,000. In the detergent-free solution, in contrast, it had a much higher molecular weight, indicating its association in forming large aggregates. The pH optimum was 9.0 when pyrophosphate buffer was used. The enzyme was active toward various aliphatic aldehydes with more than three carbons. The Km value for substrate seemed to decrease with increase in the chain length. The microsomal aldehyde dehydrogenase was not affected by disulfiram and MgCl2, which were, in contrast, highly inhibitory towards the activity of the cytosolic aldehyde dehydrogenase separated from intestinal mucosa.

References

Jan 1, 1984·Journal of Neurochemistry·H Weiner, B Ardelt
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Jun 28, 2006·The Journal of Physical Chemistry. B·Xiaojuan FanScott R J Oliver
Jun 6, 2013·Journal of Agricultural and Food Chemistry·Klaus G NeumüllerHarry Gruppen

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Citations

Jan 1, 1992·Journal of Inherited Metabolic Disease·T L KelsonW B Rizzo
Aug 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·P F JamesR A Zoeller
Nov 13, 2007·Applied and Environmental Microbiology·Yin-Ru ChiangGeorg Fuchs
Jan 27, 1998·Biochemical and Molecular Medicine·W B RizzoV De Laurenzi
Jun 23, 2011·Dermato-endocrinology·William B Rizzo

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