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...

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Published in:Canadian Journal of Zoology
Main Author: Aleksiuk, Michael
Format: Article in Journal/Newspaper
Language:English
Published: Canadian Science Publishing 1973
Subjects:
Online Access:http://dx.doi.org/10.1139/z73-082
http://www.nrcresearchpress.com/doi/pdf/10.1139/z73-082
id crcansciencepubl:10.1139/z73-082
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spelling 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
institution 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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