dc.contributor.author |
Loomes, KM |
|
dc.contributor.author |
Kitson, TM |
|
dc.coverage.spatial |
Netherlands |
|
dc.date.accessioned |
2022-06-13T04:06:37Z |
|
dc.date.available |
2022-06-13T04:06:37Z |
|
dc.date.issued |
1989-09 |
|
dc.identifier.citation |
(1989). Biochimica et Biophysica Acta: international journal of biochemistry and biophysics, 998(1), 1-6. |
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dc.identifier.issn |
0006-3002 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59786 |
|
dc.description.abstract |
The effect of various thiol-modifying reagents on the esterase activity of sheep liver cytoplasmic aldehyde dehydrogenase is reported here. Both symmetrical reagents (disulfiram, 2,2'- and 4,4'-dithiodipyridines) and unsymmetrical reagents (methyl diethylthiocarbamyl disulphide, methyl 2- and 4-pyridyl disulphides) were investigated. The results suggest that all the modifiers react to varying extents with a pair of enzymic thiol groups ('A' and 'B'), and that the more specifically group 'A' is modified, the more the enzyme is inactivated. This supports the idea that group 'A' may be the essential nucleophile in the reaction catalysed by aldehyde dehydrogenase. Modification of group 'B' may or may not reduce the esterase activity depending on the nature of the label introduced. The results of the present experiments and of previous similar experiments concerning the dehydrogenase activity of the enzyme are consistent with the proposal that a common active site is responsible for both esterase and dehydrogenase activities. |
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dc.format.medium |
Print |
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dc.language |
eng |
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dc.publisher |
Elsevier BV |
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dc.relation.ispartofseries |
Biochimica et biophysica acta |
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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 |
Liver |
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dc.subject |
Animals |
|
dc.subject |
Sheep |
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dc.subject |
Disulfides |
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dc.subject |
Thiocarbamates |
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dc.subject |
Ditiocarb |
|
dc.subject |
Disulfiram |
|
dc.subject |
Sulfhydryl Compounds |
|
dc.subject |
Pyridines |
|
dc.subject |
Esterases |
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dc.subject |
Aldehyde Dehydrogenase |
|
dc.subject |
Binding Sites |
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dc.subject |
Catalysis |
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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 |
Biophysics |
|
dc.subject |
1103 Clinical Sciences |
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dc.subject |
02 Physical Sciences |
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dc.subject |
06 Biological Sciences |
|
dc.title |
Studies of the action of symmetrical and mixed disulphide thiol-modifying reagents on the esterase activity of cytoplasmic aldehyde dehydrogenase. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1016/0167-4838(89)90110-6 |
|
pubs.issue |
1 |
|
pubs.begin-page |
1 |
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pubs.volume |
998 |
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dc.date.updated |
2022-05-03T05:16:38Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
2551390 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/2551390 |
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pubs.end-page |
6 |
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pubs.publication-status |
Published |
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dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Journal Article |
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pubs.elements-id |
128871 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
pubs.org-id |
Science Research |
|
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
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dc.identifier.eissn |
1878-2434 |
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dc.identifier.pii |
0167-4838(89)90110-6 |
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pubs.record-created-at-source-date |
2022-05-03 |
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