Cellular site in Bacillus subtilis of a nuclease which preferentially degrades single-stranded nucleic acids.
Birnboim, H. C. (Albert Einstein College of Medicine, New York, N.Y.). Cellular site in Bacillus subtilis of a nuclease which preferentially degrades single-stranded nucleic acids. J. Bacteriol. 91:1004-1011. 1966.-A nuclease, identified by a marked preference for single-stranded nucleic acids, has been demonstrated in extracts of Bacillus subtilis. The enzyme was associated with the cell wall-membrane fraction of mechanically disrupted cells and was released from cells which had been converted to protoplasts by lysozyme. The nuclease activity prepared by the latter procedure was found to be activated and solubilized by treatment with trypsin. The enzyme had about 2% activity on native deoxyribonucleic acid (DNA) as compared with denatured DNA. By use of CsCl analytical density gradient ultracentrifugation, this preparation was shown to degrade denatured DNA selectively in mixtures of native and denatured DNA.
D001412:Bacillus subtilis / Q000201:enzymology*; D002118:Calcium / Q000378:metabolism; D002845:Chromatography; D004796:Clinical Enzyme Tests; D004269:DNA, Bacterial / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009113:Muramidase; D009708:Nucleotidases / Q000494:pharmacology*; D014357:Trypsin / Q000494:pharmacology; D014461:Ultracentrifugation
D004269:DNA, Bacterial; D009708:Nucleotidases; D009113:Muramidase; D014357:Trypsin; D002118:Calcium