dc.contributor.author |
Loomes, KM |
|
dc.contributor.author |
Kitson, TM |
|
dc.coverage.spatial |
England |
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dc.date.accessioned |
2022-06-19T22:51:11Z |
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dc.date.available |
2022-06-19T22:51:11Z |
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dc.date.issued |
1989-07 |
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dc.identifier.citation |
(1989). Biochemical Journal, 261(1), 281-284. |
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dc.identifier.issn |
0264-6021 |
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dc.identifier.uri |
https://hdl.handle.net/2292/59996 |
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dc.description.abstract |
Sheep liver mitochondrial aldehyde dehydrogenase reacts with 2,2'-dithiodipyridine and 4,4'-dithiodipyridine in a two-step process: an initial rapid labelling reaction is followed by slow displacement of the thiopyridone moiety. With the 4,4'-isomer the first step results in an activated form of the enzyme, which then loses activity simultaneously with loss of the label (as has been shown to occur with the cytoplasmic enzyme). With 2,2'-dithiodipyridine, however, neither of the two steps of the reaction has any effect on the enzymic activity, showing that the mitochondrial enzyme possesses two cysteine residues that must be more accessible or reactive (to this reagent at least) than the postulated catalytically essential residue. The symmetrical reagent 5,5'-dithiobis-(1-methyltetrazole) activates mitochondrial aldehyde dehydrogenase approximately 4-fold, whereas the smaller related compound methyl l-methyltetrazol-5-yl disulphide is a potent inactivator. These results support the involvement of mixed methyl disulphides in causing unpleasant physiological responses to ethanol after the ingestion of certain antibiotics. |
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dc.format.medium |
Print |
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dc.language |
eng |
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dc.publisher |
Portland Press Ltd. |
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dc.relation.ispartofseries |
The Biochemical journal |
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dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
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dc.subject |
Mitochondria, Liver |
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dc.subject |
Animals |
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dc.subject |
Sheep |
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dc.subject |
Disulfides |
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dc.subject |
Tetrazoles |
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dc.subject |
Pyridines |
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dc.subject |
2,2'-Dipyridyl |
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dc.subject |
Aldehyde Dehydrogenase |
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dc.subject |
Sulfhydryl Reagents |
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dc.subject |
Enzyme Activation |
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dc.subject |
Aging |
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dc.subject |
Alcoholism, Alcohol Use and Health |
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dc.subject |
Substance Abuse |
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dc.subject |
Digestive Diseases |
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dc.subject |
Rare Diseases |
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dc.subject |
Liver Disease |
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dc.subject |
Science & Technology |
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dc.subject |
Life Sciences & Biomedicine |
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dc.subject |
Biochemistry & Molecular Biology |
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dc.subject |
0601 Biochemistry and Cell Biology |
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dc.subject |
Clinical Medicine and Science |
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dc.subject |
03 Chemical Sciences |
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dc.subject |
06 Biological Sciences |
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dc.subject |
11 Medical and Health Sciences |
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dc.title |
Reaction between sheep liver mitochondrial aldehyde dehydrogenase and various thiol-modifying reagents. |
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dc.type |
Journal Article |
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dc.identifier.doi |
10.1042/bj2610281 |
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pubs.issue |
1 |
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pubs.begin-page |
281 |
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pubs.volume |
261 |
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dc.date.updated |
2022-05-05T02:03:40Z |
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dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
2775216 (pubmed) |
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pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/2775216 |
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pubs.end-page |
284 |
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pubs.publication-status |
Published |
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dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
research-article |
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pubs.subtype |
Journal Article |
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pubs.elements-id |
128855 |
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pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
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pubs.org-id |
Science Research |
|
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
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dc.identifier.eissn |
1470-8728 |
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pubs.record-created-at-source-date |
2022-05-05 |
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