Separation of ATP-dependent DNAse to ATPase and DNAse.
A 250-fold purified ATP-dependent DNase from Bacillus cereus has been separated to DNA-dependent ATPase I and II and a DNase specific for single-stranded DNA (ssDNase) by means of high resolution of DEAE cellulose chromatography. Simultaneously with the separation of ATPase and ssDNase, a decrease in ATP-dependent DNase activity was observed. Complete separation resulted in the total loss of ATP-dependent DNase activity. Reconstitution of ATP-stimulated DNase activity was dependent on the ratio of the combined ATPase II and ssDNase.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D001409:Bacillus cereus / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D004247:DNA / Q000494:pharmacology; D004277:DNA, Single-Stranded / Q000378:metabolism; D003851:Deoxyribonucleases / Q000302:isolation & purification*; D006358:Hot Temperature; D009691:Nucleic Acid Denaturation; D013379:Substrate Specificity
D004277:DNA, Single-Stranded; D000255:Adenosine Triphosphate; D004247:DNA; D003851:Deoxyribonucleases; D000251:Adenosine Triphosphatases