Effect of cobalt on synthesis and activation of Bacillus licheniformis alkaline phosphatase.
AUTOR(ES)
Spencer, D B
RESUMO
The effect of CO2+ on the synthesis and activation of Bacillus licheniformis MC14 alkaline phosphatase has been shown by the development of a defined minimal salts medium in which this organism produces 35 times more (assayable) alkaline phosphatase than when grown in a low-phosphate complex medium or in the defined medium without cobalt. Stimulation of enzyme activity with cobalt is dependent on a low phosphate concentration in the medium (below 0.075 mM) and continued protein synthesis. Cobalt stimulation resulted in alkaline phosphate production being a major portion of total protein synthesized during late-logarithmic and early-stationary-phase culture growth. Cells cultured in the defined medium minus cobalt, or purified enzyme partially inactivated with a chelating agent, showed a 2.5-fold increase in activity when assayed in the presence of cobalt. Atomic spectral analysis indicated the presence of 3.65 +/- 0.45 g-atoms of cobalt associated with each mole of purified active alkaline phosphatase. A biochemical localization as a function of culture age in this medium showed that alkaline phosphatase was associated with the cytoplasmic membrane and was also found as a soluble enzyme in the periplasmic region and secreted into the growth medium.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=217200Documentos Relacionados
- Cloning and characterization of the Bacillus licheniformis gene coding for alkaline phosphatase.
- Cobalt(III), a probe of metal binding sites of Escherichia coli alkaline phosphatase.
- Alkaline phosphatase secretion-negative mutant of Bacillus licheniformis 749/C.
- Subunits of the alkaline phosphatase of Bacillus licheniformis: chemical, physicochemical, and dissociation studies.
- Electron microscope histochemical localization of alkaline phosphatase(s) in Bacillus licheniformis.
