Binding of the ATP-dependent DNase from Hemophilus influenzae to duplex DNA molecules.
Using a membrane filter assay, we have studied the binding reaction between the ATP-dependent DNase from Hemophilus influenzae and duplex DNA under conditions where the degradative reaction is not allowed to proceed. Experiments with three forms of SV40 DNA. Complex formation between enzyme and DNA requires neither DNA or enzyme concentration is fixed while the other is varied reveal that binding is noncooperative and that there are two binding sites per linear DNA molecule. These binding sites probably correspond to the two termini of the molecule.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D004269:DNA, Bacterial; D003851:Deoxyribonucleases / Q000378:metabolism*; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D006193:Haemophilus influenzae / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008433:Mathematics
D004269:DNA, Bacterial; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D003851:Deoxyribonucleases; D008274:Magnesium; D004121:Dimethyl Sulfoxide