Selenium as Inducer of Glutathione Peroxidase in low-CO2-Grown Chlamydomonas reinhardtii1
AUTOR(ES)
Yokota, Akiho
RESUMO
Culture of the green alga Chlamydomonas reinhardtii in the medium containing sodium selenite caused the activity of ascorbate peroxidase to disappear and the appearance of glutathione peroxidase. The induced maximum activity of glutathione peroxidase reached 350 micromole (milligram chlorophyll hour)−1 under assay conditions used. The enzymic properties of the selenite-induced glutathione peroxidase closely resembled those of animal glutathione peroxidase that contains selenium.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1054545Documentos Relacionados
- A low-CO2-inducible gene encoding an alanine: alpha-ketoglutarate aminotransferase in Chlamydomonas reinhardtii.
- Induction and Regulation of Expression of a Low-CO2-Induced Mitochondrial Carbonic Anhydrase in Chlamydomonas reinhardtii
- Active CO2 Transport by the Green Alga Chlamydomonas reinhardtii1
- Rubisco Activase Is Required for Optimal Photosynthesis in the Green Alga Chlamydomonas reinhardtii in a Low-CO2 Atmosphere1
- Effect of CO2 Concentration on Protein Biosynthesis and Carbonic Anhydrase Expression in Chlamydomonas reinhardtii1
