Phosphorescence of alkaline phosphatase of E. coli in vitro and in situ.
Escherichia coli K-12, which is rich in alkaline phosphatase, exhibits phosphorescence characteristic of tryptophan at room temperature. E coli mutants which do not have alkaline phosphatase do not show long-lived phosphorescence. The phosphorescence spectrum and lifetime of E. coli K-12 was similar to that of purified alkaline phosphatase from E. coli. These results indicate that the long-lived tryptophan phosphorescence in E. coli is likely to be derived from alkaline phosphatase in situ. The temperature dependence of tryptophan phosphorescence life-time of purified alkaline phosphatase and E. coli K-12 differ; this may imply that alkaline phosphatase in E. coli may be associated with the cell envelope and is therefore protected against structural changes in the protein which result in increased phosphorescence decay rates.
D000469:Alkaline Phosphatase; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007700:Kinetics; D008163:Luminescent Measurements; D009154:Mutation; D013045:Species Specificity; D013057:Spectrum Analysis; D013696:Temperature; D014364:Tryptophan
D014364:Tryptophan; D000469:Alkaline Phosphatase