Cytochemical studies on alkaline phosphatase production during sporulation in Bacillus subtilis.
During sporulation of Bacillus subtilis 168 there is an increase in activity of alkaline phosphatase in the presence of Pi. This enzyme was shown by cytochemical techniques to be associated with the cytoplasmic membrane of the mother cell and also with the membranes of the developing prespore. There is a strong correlation between an increasing number of electron-dense deposits due to phosphatase activity and the formation of the spore septum, i.e. stage II of sporulation. Cytochemical and biochemical evidence shows that cells well advanced in spore formation can be derepressed to produce the very much higher amounts of alkaline phosphatase characteristic of phosphate-starved vegetative cells.
D000469:Alkaline Phosphatase / Q000096:biosynthesis*; D001412:Bacillus subtilis / Q000032:analysis / Q000201:enzymology* / Q000648:ultrastructure; D002462:Cell Membrane / Q000648:ultrastructure; D004789:Enzyme Activation; D006651:Histocytochemistry; D008854:Microscopy, Electron; D010710:Phosphates / Q000494:pharmacology; D013171:Spores, Bacterial / Q000201:enzymology / Q000648:ultrastructure
D010710:Phosphates; D000469:Alkaline Phosphatase