Purificación de Tiorredoxina reductasa de mamifero
Fecha
2021-07-29
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Jaén: Universidad de Jaén
Resumen
[ES] La Tioredoxina reductasa (TRR) es una enzima oxido‐reductasa que transfiere los electrones del NADPH
a la tiorredoxina. A su vez, la tiorredoxina reduce enlaces disulfuro en una variedad de proteínas, entre
ellas las peroxirredoxinas, que reducen el peróxido de hidrógeno a agua. Por tanto, la tiorredoxina
reductasa participa en la defensa antioxidante de las células. La TRR de mamíferos es una selenoproteína
y su residuo de selenocisteína es esencial para la actividad de la enzima. Hoy día, la purificación de
proteínas se realiza mayoritariamente a través de la expresión de ADN recombinante en bacterias, pero
las bacterias carecen de los mecanismos para incorporar selenocisteína a las proteínas. Por este motivo,
en este trabajo se ha tratado de purificar TRR a partir de hígado de mamífero (cordero) por cromatografía
líquida.
[EN] Thioredoxin reductase (TRR) is an oxido‐reductase enzyme that transfers electrons from NADPH to thioredoxin. In turn, thioredoxin reduces disulfide bonds in a variety of proteins, including peroxiredoxins, which reduce hydrogen peroxide to water. Therefore, thioredoxin reductase participates in the antioxidant defense of cells. Mammalian TRR is a selenoprotein and its selenocysteine residue is essential for enzyme activity. Today, protein purification is mostly done through the expression of recombinant DNA in bacteria, but bacteria lack the mechanisms to incorporate selenocysteine into proteins. For this reason, in this work we have tried to purify TRR from mammalian (lamb) liver by liquid chromatography.
[EN] Thioredoxin reductase (TRR) is an oxido‐reductase enzyme that transfers electrons from NADPH to thioredoxin. In turn, thioredoxin reduces disulfide bonds in a variety of proteins, including peroxiredoxins, which reduce hydrogen peroxide to water. Therefore, thioredoxin reductase participates in the antioxidant defense of cells. Mammalian TRR is a selenoprotein and its selenocysteine residue is essential for enzyme activity. Today, protein purification is mostly done through the expression of recombinant DNA in bacteria, but bacteria lack the mechanisms to incorporate selenocysteine into proteins. For this reason, in this work we have tried to purify TRR from mammalian (lamb) liver by liquid chromatography.