Open AccessSelenium as Inducer of Glutathione Peroxidase in low-CO2-Grown Chlamydomonas reinhardtii
Author(s) -
Akiho Yokota,
Shigeru Shigeoka,
Toshio Onishi,
Shôzaburo Kitaoka
Publication year - 1988
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.86.3.649
Subject(s) - chlamydomonas reinhardtii , peroxidase , selenium , glutathione peroxidase , glutathione , gpx3 , biochemistry , chemistry , chlamydomonas , enzyme , organic chemistry , mutant , gene
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.