Purification and characterisation of Bst LVI restriction endonuclease, a thermostable isoschizomer of ClaI from Bacillus stearothermophilus LV

Biochim Biophys Acta. 1993 Jan 23;1171(3):295-8. doi: 10.1016/0167-4781(93)90068-o.

Abstract

This work describes the purification and biochemical characterization of BstLVI restriction endonuclease, a thermostable isoschizomer of ClaI, from Bacillus stearothermophilus LV. The enzyme was purified by successive DEAE-cellulose, Affi-Gel Blue and Heparin-Sepharose CL-6B column chromatography. A molecular weight of 37,000 was determined for Bst LVI by gel filtration. As expected from thermophilic proteins, the enzyme showed a high stability towards heat and also to other known protein-denaturing agents.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA / metabolism
  • Deoxyribonucleases, Type II Site-Specific / chemistry
  • Deoxyribonucleases, Type II Site-Specific / isolation & purification*
  • Deoxyribonucleases, Type II Site-Specific / metabolism
  • Enzyme Stability
  • Geobacillus stearothermophilus / enzymology*
  • Substrate Specificity

Substances

  • DNA
  • ATCGAT-specific type II deoxyribonucleases
  • Deoxyribonucleases, Type II Site-Specific