Specific release of plasma membrane enzymes by a phosphatidylinositol-specific phospholipase C.
The release of plasma membrane ecto-enzymes by a phosphatidylinositol-specific phospholipase C from Staphylococcus aureus was investigated. There was no effect on L-leucyl-beta-naphthylamidase, alkaline phosphodeisterase I and Ca2+- or MG2+-ATPase, but substantial proportions of the alkaline phosphatase and 5-nucleotidase were released. There was no simultaneous release of phospholipid and the solubilized enzymes were not exluded from Sepharose 6-B. It was therefore concluded that release was not a secondary consequence of membrane vesiculation but occurred as a result of the disruption of specific interactions involving the phosphatidylinositol molecule.
D000251:Adenosine Triphosphatases; D000469:Alkaline Phosphatase; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D007931:Leucyl Aminopeptidase; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D009708:Nucleotidases; D010716:Phosphatidylinositols; D010740:Phospholipases / Q000378:metabolism*; D010727:Phosphoric Diester Hydrolases; D051381:Rats; D013211:Staphylococcus aureus / Q000201:enzymology*
D010716:Phosphatidylinositols; D010740:Phospholipases; D009708:Nucleotidases; D000469:Alkaline Phosphatase; D010727:Phosphoric Diester Hydrolases; D007931:Leucyl Aminopeptidase; D000251:Adenosine Triphosphatases