Surface-bound nuclease of Stapylococcus aureus: purification and properties of the enzymes.
The surface-bound nuclease of Staphylococcus aureus liberated during formation of protoplasts was purified 1,000-fold by chromatography on phosphocellulose. Its properties were compared with those of the known extracellular nuclease, purified 200-fold by the same procedures. The adsorbance of the surface-bound nuclease on phosphocellulose was distinctly different from that of the extracellular nuclease, but other properties of the two enzymes were similar. Both enzymes had a pH optimum of about 10 and required Ca(2+) for activity. Both enzymes hydrolyzed deoxyribonucleic acid (DNA) and ribonucleic acid, and denatured DNA was a better substrate than native DNA. Both enzymes were inhibited by the same metal ions. Nuclease-less mutants of S. aureus were isolated from S. aureus 209P by using N-methyl-N'-nitroso-N-nitrosoguanidine. These mutants contained neither surface-bound nor extracellular nuclease activity. These results suggest that the surface-bound and extracellular nucleases are expressed from the same cistron of S. aureus.
D000645:Ammonium Sulfate; D002118:Calcium / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D002473:Cell Wall / Q000201:enzymology; D011232:Chemical Precipitation; D002852:Chromatography, Ion Exchange; D004269:DNA, Bacterial / Q000378:metabolism; D003851:Deoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism; D005092:Exonucleases / Q000378:metabolism; D005417:Flavobacterium / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D009153:Mutagens; D009154:Mutation; D009604:Nitrosoguanidines; D009691:Nucleic Acid Denaturation; D011523:Protoplasts; D013210:Staphylococcus / Q000201:enzymology*; D014316:Tritium
D004269:DNA, Bacterial; D004798:Enzymes; D009153:Mutagens; D009604:Nitrosoguanidines; D014316:Tritium; D003851:Deoxyribonucleases; D005092:Exonucleases; D000645:Ammonium Sulfate; D002118:Calcium