The ATP-dependent DNAase from Escherichia coli rorA: a nuclease with changed enzymatic properties.
The ATP-dependent DNAases from Escherichia coli wild-type and rorA were isolated and purified and their enzymatic properties were compared. The enzymes were found to differ in the amount of ATP that is consumed during DNA degradation. This difference can be influenced by the reaction conditions and the nature of the substrate.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004247:DNA / Q000528:radiation effects; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D009154:Mutation; D009994:Osmolar Concentration; D011830:Radiation Effects; D012910:Snake Venoms; D012965:Sodium Chloride / Q000494:pharmacology; D013045:Species Specificity; D013997:Time Factors; D014466:Ultraviolet Rays
D012910:Snake Venoms; D012965:Sodium Chloride; D000255:Adenosine Triphosphate; D004247:DNA; D003851:Deoxyribonucleases