Elevation of superoxide dismutase in Halobacterium halobium by heat shock.
AUTOR(ES)
Begonia, G B
RESUMO
Exposure of Halobacterium halobium to 50 degrees C for 2.5 h in an aerobic environment resulted in a greater than twofold increase in the activity of the manganese-containing superoxide dismutase. Nondenaturing polyacrylamide gels stained for enzymatic activity did not reveal any additional isozymes of superoxide dismutase induced by the heat shock. The maximal effect was observed at 50 degrees C, and the elevated levels of activity remained constant during 5 h of recovery at 40 degrees C. The induction of enzymatic activity was sensitive to protein synthesis inhibitors. The results are discussed relative to heat shock and stress-related proteins as well as alterations in metabolism brought about by elevated temperatures.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=208277Documentos Relacionados
- Induction of superoxide dismutase in Escherichia coli by heat shock.
- Tandem arrangement of photolyase and superoxide dismutase genes in Halobacterium halobium.
- Superoxide dismutase protects against aerobic heat shock in Escherichia coli.
- Alternative 5' splice site selection induced by heat shock.
- Superoxide dismutase from the extremely halophilic archaebacterium Halobacterium cutirubrum.