A manganese-stimulated endonuclease from Bacillus subtilis

B. Scher, D. Dubnau

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

An endonuclease activity has been identified in extracts of Bacillus subtilis. This activity is stimulated by Mn++ or Ca++ ions but not by Mg++ ions. The enzyme catalyzes the breakdown of native DNA of high molecular weight to fragments of molecular weights ranging from 3 × 106 to 20 × 106. A variety of DNA's from sources such as B. subtilis, Salmonella and T7 phage are attacked. About 61% of the activity of the cells is released into the medium during protoplast formation under conditions where 98% of the glucose 6-P dehydrogenase activity is retained by the cells.

Original languageEnglish (US)
Pages (from-to)595-602
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume55
Issue number3
DOIs
StatePublished - Dec 10 1973

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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