Cytochemistry of phosphatases in Myxococcus xanthus.
An Mg(2+)-dependent and a K(+)-stimulated adenosine triphosphatase were localized by cytochemistry at or near both surfaces of the cytoplasmic membrane of Myxococcus xanthus. An alkaline and an acid phosphatase resided at the external surface of the membrane or in the periplasm. All enzymes could be extracted from partially fixed cells with Mg(2+)-deficient buffers. Suboptimal external phosphate elicited dissociation of adenosine triphosphatase from the membrane but not that of the unspecific phosphatases. The dissociated enzymes migrated into the cytoplasm where they were associated mainly with cytoplasmic aggregates.
D000135:Acid Phosphatase; D000251:Adenosine Triphosphatases; D000469:Alkaline Phosphatase; D001419:Bacteria / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D006651:Histocytochemistry; D008274:Magnesium / Q000494:pharmacology; D008566:Membranes / Q000201:enzymology; D008854:Microscopy, Electron; D011188:Potassium / Q000494:pharmacology
D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium