Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta )
The electrophoretic patterns and temperature-dependent kinetics of cytoplasmic malate dehydrogenase from liver of juvenile and adult representatives of the common crow (Corvus brachyrhynchos), an altricial species, and the pintail (Anus acuta), a precocial species, were examined. Starch gel electrop...
Published in: | Canadian Journal of Zoology |
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Canadian Science Publishing
1973
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Online Access: | http://dx.doi.org/10.1139/z73-082 http://www.nrcresearchpress.com/doi/pdf/10.1139/z73-082 |
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crcansciencepubl:10.1139/z73-082 2023-12-17T10:18:26+01:00 Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) Aleksiuk, Michael 1973 http://dx.doi.org/10.1139/z73-082 http://www.nrcresearchpress.com/doi/pdf/10.1139/z73-082 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Canadian Journal of Zoology volume 51, issue 6, page 557-565 ISSN 0008-4301 1480-3283 Animal Science and Zoology Ecology, Evolution, Behavior and Systematics journal-article 1973 crcansciencepubl https://doi.org/10.1139/z73-082 2023-11-19T13:38:38Z The electrophoretic patterns and temperature-dependent kinetics of cytoplasmic malate dehydrogenase from liver of juvenile and adult representatives of the common crow (Corvus brachyrhynchos), an altricial species, and the pintail (Anus acuta), a precocial species, were examined. Starch gel electrophoresis revealed two major isoenzymes in each case. The isoenzymes of the juvenile and adult crow exhibit different electrophoretic mobilities, while those of the juvenile and adult pintail exhibit identical mobilities. Assay temperature has no statistically significant age-specific or species-specific effects on several kinetic properties of malate dehydrogenase. In all cases, the Michaelis constant (K m ) of oxaloacetate for malate dehydrogenase remains fairly stable below 15 °C, but increases three- to four-fold from 15 ° to 45 °C. Values of activation energy vary between 12.1 and 15.0 kcal/mol. Q 10 values for reaction velocities at minimum K m substrate levels are about 1.0 between 30° and 40 °C. The adaptive significance of the observed effects is discussed in relation to poikilothermic stages of the early posthatching ontogeny of birds. Article in Journal/Newspaper Anas acuta Canadian Science Publishing (via Crossref) Canadian Journal of Zoology 51 6 557 565 |
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Open Polar |
collection |
Canadian Science Publishing (via Crossref) |
op_collection_id |
crcansciencepubl |
language |
English |
topic |
Animal Science and Zoology Ecology, Evolution, Behavior and Systematics |
spellingShingle |
Animal Science and Zoology Ecology, Evolution, Behavior and Systematics Aleksiuk, Michael Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) |
topic_facet |
Animal Science and Zoology Ecology, Evolution, Behavior and Systematics |
description |
The electrophoretic patterns and temperature-dependent kinetics of cytoplasmic malate dehydrogenase from liver of juvenile and adult representatives of the common crow (Corvus brachyrhynchos), an altricial species, and the pintail (Anus acuta), a precocial species, were examined. Starch gel electrophoresis revealed two major isoenzymes in each case. The isoenzymes of the juvenile and adult crow exhibit different electrophoretic mobilities, while those of the juvenile and adult pintail exhibit identical mobilities. Assay temperature has no statistically significant age-specific or species-specific effects on several kinetic properties of malate dehydrogenase. In all cases, the Michaelis constant (K m ) of oxaloacetate for malate dehydrogenase remains fairly stable below 15 °C, but increases three- to four-fold from 15 ° to 45 °C. Values of activation energy vary between 12.1 and 15.0 kcal/mol. Q 10 values for reaction velocities at minimum K m substrate levels are about 1.0 between 30° and 40 °C. The adaptive significance of the observed effects is discussed in relation to poikilothermic stages of the early posthatching ontogeny of birds. |
format |
Article in Journal/Newspaper |
author |
Aleksiuk, Michael |
author_facet |
Aleksiuk, Michael |
author_sort |
Aleksiuk, Michael |
title |
Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) |
title_short |
Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) |
title_full |
Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) |
title_fullStr |
Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) |
title_full_unstemmed |
Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( Corvus brachyrhynchos ) and the pintail ( Anas acuta ) |
title_sort |
temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow ( corvus brachyrhynchos ) and the pintail ( anas acuta ) |
publisher |
Canadian Science Publishing |
publishDate |
1973 |
url |
http://dx.doi.org/10.1139/z73-082 http://www.nrcresearchpress.com/doi/pdf/10.1139/z73-082 |
genre |
Anas acuta |
genre_facet |
Anas acuta |
op_source |
Canadian Journal of Zoology volume 51, issue 6, page 557-565 ISSN 0008-4301 1480-3283 |
op_rights |
http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/z73-082 |
container_title |
Canadian Journal of Zoology |
container_volume |
51 |
container_issue |
6 |
container_start_page |
557 |
op_container_end_page |
565 |
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1785563778853634048 |