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Aquino-Silva,Maria Regina de; Schwantes,Maria Luiza Barcellos; Munin,Flavia Simone; Schwantes,Arno Rudi; Santos,Silvana Pereira dos. |
Kinetic properties and thermal stabilities of Geophagus brasiliensis skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to examine a possible sMDH-B* locus duplication in a fixation process influenced by genetic drift. Two optimal pHs were detected: 7.5 for AB1 unfractionated muscle phenotype and its B1 isoform, and 8.0 for AB1B2 unfractionated muscle phenotype, A and B2 isoforms. While G. brasiliensis A isoform could be characterized as thermostable, the duplicated B isoform cannot be assumed as thermolabile. Km values for isolated B2 isoforms were 1.6 times lower than for B1. A duplication event in progress best explains the electrophoretic six-band pattern detected in G. brasiliensis, which... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Gene duplication; SMDH; Substrate concentration; Temperature; PH isoforms. |
Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000200029 |
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Monteiro,Maria do Carmo; Schwantes,Maria Luiza B.; Schwantes,Arno Rudi; Silva,Maria Regina de Aquino. |
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... |
Tipo: Info:eu-repo/semantics/article |
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Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47571998000200004 |
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Aquino-Silva,Maria Regina de; Schwantes,Maria Luiza B.; Schwantes,Arno Rudi. |
A recent locus duplication hypothesis for sMDH-B* was proposed to explain the complex electrophoretic pattern of six bands detected for the soluble form of malate dehydrogenase (MDH, EC 1.1.1.37) in 84% of the Geophagus brasiliensis (Cichlidae, Perciformes) analyzed (AB1B2 individuals). Klebe's serial dilutions were carried out in skeletal muscle extracts. B1 and B2 subunits had the same visual end-points, reflecting a nondivergent pattern for these B-duplicated genes. Since there is no evidence of polyploidy in the Cichlidae family, MDH-B* loci must have evolved from regional gene duplication. Tissue specificities, thermostability and kinetic tests resulted in similar responses from both B-isoforms, in both sMDH phenotypes, suggesting that these more... |
Tipo: Info:eu-repo/semantics/article |
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Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47571998000400016 |
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Santos,Marcelo dos; Schwantes,Maria Luiza B.; Schwantes,Arno Rudi. |
The scale number in lateral sets (SNS) of Mugil sp. (Mugilidae, Perciformes) collected in the lagoon-estuarine region of Cananéia, State of São Paulo ranges from 33 to 39. Electrokinetic, kinetic and thermostability properties of lactate dehydrogenase (LDH) were tested to determine if individuals with different SNS correspond to different species or populations of mullet. As in many other teleosts, LDH-A*, LDH-B*, and LDH-C* loci were detected. Through a two-fold serial dilution method applied to 10 different tissues of Mugil sp., a bidirectionally divergent expression of these loci was suggested. No association among LDH electrophoretic pattern, thermal inactivation, kinetic responses and different SNS was observed. The apparent Km (pyr) values obtained... |
Tipo: Info:eu-repo/semantics/article |
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Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572000000100026 |
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