Trematomus Newnesi
Mostrando 1-4 de 4 artigos, teses e dissertações.
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1. Movimento retinomotor do peixe antártico Trematomus newnesi Boulenger submetido a diferentes condições fóticas
O peixe antártico Trematoms newnesi (Boulenger, 1902) vive em habitats benticos à pelágicos, em condições fóticas que variam sazonalmente e diariamente, induzindo os movimentos retinomotores. Peixes foram mantidos experimentalmente, durante sete dias, sob luz ou escuro constante, e 12 horas luz/12 horas escuro. O movimento retinomotor do epitélio pigm
Revista Brasileira de Zoologia. Publicado em: 2007-06
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2. Análise das respostas citogenotóxicas e histopatológicas do peixe Trematomus newnesi exposto à água do mar diante da Estação Antártica Brasileira "Comandante Ferraz", Ilha Rei George, Antártica / Analysis of cytogenotoxic and histopathologic responses of the fish Trematomus newnesi exposed to seawater in front of the Brazilian Antarctic Research Station "Comandandante Ferraz", King George Island, Antarctica.
Many countries have installed research stations in Antarctica. Petroleum hydrocarbons and the sewage disposed into the sea by the stations are potential sources of pollution in Antarctica. Trematomus newnesi specimens were used to assess genotoxic potential and histopathology of the liver and gills of the water surrounding the Brazilian Antarctic Station ?Co
Publicado em: 2007
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3. Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins
Oxidation of Hbs leads to the formation of different forms of Fe(III) that are relevant to a range of biochemical and physiological functions. Here we report a combined EPR/x-ray crystallography study performed at acidic pH on six ferric tetrameric Hbs. Five of the Hbs were isolated from the high-Antarctic notothenioid fishes Trematomus bernacchii, Trematom
The Biophysical Society.
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4. The crystal structure of a tetrameric hemoglobin in a partial hemichrome state
Tetrameric hemoglobins are the most widely used systems in studying protein cooperativity. Allosteric effects in hemoglobins arise from the switch between a relaxed (R) state and a tense (T) state occurring upon oxygen release. Here we report the 2.0-Å crystal structure of the main hemoglobin component of the Antarctic fish Trematomus newnesi, in a partial
The National Academy of Sciences.