[Effect of detergents and proteolytic enzymes on membrane-bound phosphohydrolases in Escherichia coli cells with repressed and depressed biosynthesis of these enzymes].
Solubilization of protein membranes by detergents and protein liberation from the membranes induced by proteolytic enzymes results in a change of activity of membrane-bound phosphohydrolases--alkaline phosphatase and polyphosphatase. The activity of enzymes under conditions of repressed and derepressed biosynthesis of phosphohydrolases changes differently, thus indicating their different membrane environment in the two types of membranes. Some data were obtained on the localization of alkaline phosphatase in a hydrophobic region, possibly in lipid bilayer and polyphosphatase in the surface layers of the membrane.
D001665:Binding Sites; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D008854:Microscopy, Electron; D010206:Papain / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011402:Pronase / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
D003902:Detergents; D003840:Deoxycholic Acid; D010744:Phosphoric Monoester Hydrolases; D010447:Peptide Hydrolases; D014357:Trypsin; D010206:Papain; D011402:Pronase
Deĭstvie detergentov i protsoliticheskikh fermentov na membranosviazannye fosfogidrolazy v kletkakh Escherichia coli s repressirovannym i depressirovannym biosintezom étikh fermentov