Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes

Detalhes bibliográficos
Autor(a) principal: Monteiro,Maria do Carmo
Data de Publicação: 1998
Outros Autores: Schwantes,Maria Luiza B., Schwantes,Arno Rudi, Silva,Maria Regina de Aquino
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Genetics and Molecular Biology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47571998000200004
Resumo: Electrophoretic thermostability tests of soluble malate dehydrogenases (sMDH) isozymes in tissue extracts of 21 subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes showed three distinct results. The first, characterized by thermal stability of the slowest-migrating band or A-isoform, was detected in 52% of all species. The second, exhibited in 29% of the species analyzed, had a bidirectionally divergent pattern of their sMDH locus expression, and was characterized by a nondivergent thermostability pattern of both sMDH-A* and B*. In the third category, obtained in 19% of the species studied (the four Siluriformes species), thermostability of the fastest-migrating bands, or B-isoforms, was observed. Comparison of the effects of habitat temperature on the activity of paralogous and orthologous isoforms in tissue extracts of two of these species with different thermostability properties (Leporinus friderici - thermostable sMDH-A*, and Pimelodus maculatus - reverse thermostability properties or reverse electrophoretic pattern), collected during winter and summer months, showed that A and B subunits were present at different quantitative levels and their activities were nearly season independent. Differences in susceptibility to temperature (50°C) of both sMDH loci from tissue extracts of these species were found. In P. maculatus, these susceptibilities helped strengthen one of the hypotheses: the reverse thermostability pattern, where the fastest-migrating band or the B-isoform was the thermostable sMDH. Thus, temperature differences among orthologous homologues of sMDH seem to have occurred in these acclimatized species, where the fastest-migrating band, usually muscle specific and thermolabile in most teleosts, appeared in P. maculatus as the thermostable isoform.
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spelling Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and PerciformesElectrophoretic thermostability tests of soluble malate dehydrogenases (sMDH) isozymes in tissue extracts of 21 subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes showed three distinct results. The first, characterized by thermal stability of the slowest-migrating band or A-isoform, was detected in 52% of all species. The second, exhibited in 29% of the species analyzed, had a bidirectionally divergent pattern of their sMDH locus expression, and was characterized by a nondivergent thermostability pattern of both sMDH-A* and B*. In the third category, obtained in 19% of the species studied (the four Siluriformes species), thermostability of the fastest-migrating bands, or B-isoforms, was observed. Comparison of the effects of habitat temperature on the activity of paralogous and orthologous isoforms in tissue extracts of two of these species with different thermostability properties (Leporinus friderici - thermostable sMDH-A*, and Pimelodus maculatus - reverse thermostability properties or reverse electrophoretic pattern), collected during winter and summer months, showed that A and B subunits were present at different quantitative levels and their activities were nearly season independent. Differences in susceptibility to temperature (50°C) of both sMDH loci from tissue extracts of these species were found. In P. maculatus, these susceptibilities helped strengthen one of the hypotheses: the reverse thermostability pattern, where the fastest-migrating band or the B-isoform was the thermostable sMDH. Thus, temperature differences among orthologous homologues of sMDH seem to have occurred in these acclimatized species, where the fastest-migrating band, usually muscle specific and thermolabile in most teleosts, appeared in P. maculatus as the thermostable isoform.Sociedade Brasileira de Genética1998-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47571998000200004Genetics and Molecular Biology v.21 n.2 1998reponame:Genetics and Molecular Biologyinstname:Sociedade Brasileira de Genética (SBG)instacron:SBG10.1590/S1415-47571998000200004info:eu-repo/semantics/openAccessMonteiro,Maria do CarmoSchwantes,Maria Luiza B.Schwantes,Arno RudiSilva,Maria Regina de Aquinoeng1999-01-06T00:00:00Zoai:scielo:S1415-47571998000200004Revistahttp://www.gmb.org.br/ONGhttps://old.scielo.br/oai/scielo-oai.php||editor@gmb.org.br1678-46851415-4757opendoar:1999-01-06T00:00Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG)false
dc.title.none.fl_str_mv Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
title Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
spellingShingle Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
Monteiro,Maria do Carmo
title_short Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
title_full Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
title_fullStr Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
title_full_unstemmed Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
title_sort Thermal stability of soluble malate dehydrogenase isozymes of subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes
author Monteiro,Maria do Carmo
author_facet Monteiro,Maria do Carmo
Schwantes,Maria Luiza B.
Schwantes,Arno Rudi
Silva,Maria Regina de Aquino
author_role author
author2 Schwantes,Maria Luiza B.
Schwantes,Arno Rudi
Silva,Maria Regina de Aquino
author2_role author
author
author
dc.contributor.author.fl_str_mv Monteiro,Maria do Carmo
Schwantes,Maria Luiza B.
Schwantes,Arno Rudi
Silva,Maria Regina de Aquino
description Electrophoretic thermostability tests of soluble malate dehydrogenases (sMDH) isozymes in tissue extracts of 21 subtropical fish belonging to the orders Characiformes, Siluriformes and Perciformes showed three distinct results. The first, characterized by thermal stability of the slowest-migrating band or A-isoform, was detected in 52% of all species. The second, exhibited in 29% of the species analyzed, had a bidirectionally divergent pattern of their sMDH locus expression, and was characterized by a nondivergent thermostability pattern of both sMDH-A* and B*. In the third category, obtained in 19% of the species studied (the four Siluriformes species), thermostability of the fastest-migrating bands, or B-isoforms, was observed. Comparison of the effects of habitat temperature on the activity of paralogous and orthologous isoforms in tissue extracts of two of these species with different thermostability properties (Leporinus friderici - thermostable sMDH-A*, and Pimelodus maculatus - reverse thermostability properties or reverse electrophoretic pattern), collected during winter and summer months, showed that A and B subunits were present at different quantitative levels and their activities were nearly season independent. Differences in susceptibility to temperature (50°C) of both sMDH loci from tissue extracts of these species were found. In P. maculatus, these susceptibilities helped strengthen one of the hypotheses: the reverse thermostability pattern, where the fastest-migrating band or the B-isoform was the thermostable sMDH. Thus, temperature differences among orthologous homologues of sMDH seem to have occurred in these acclimatized species, where the fastest-migrating band, usually muscle specific and thermolabile in most teleosts, appeared in P. maculatus as the thermostable isoform.
publishDate 1998
dc.date.none.fl_str_mv 1998-06-01
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dc.publisher.none.fl_str_mv Sociedade Brasileira de Genética
publisher.none.fl_str_mv Sociedade Brasileira de Genética
dc.source.none.fl_str_mv Genetics and Molecular Biology v.21 n.2 1998
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