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An efficient method to eliminate the protease activity contaminating commercial bovine pancreatic DNase I.

Abstract
A method was developed to eliminate the proteases contaminating commercial DNase I, which can cause degradation of target protein during the purification process. Bio Basic DNase stock solution (in Tris-HCl buffer [pH 8.0] containing 5mM CaCl2) was first incubated at 50 °C to generate autolysis of proteases and zymogens, leading to a significant reduction in protease activity while preserving DNase activity. The residual protease activity was completely inhibited by further incubation with 2mM PMSF (phenylmethylsulfonyl fluoride) or 2× S8830 inhibitor cocktail. This approach could be readily applicable to eliminate the protease activity in any DNase products or during the preparation of commercial DNase.
AuthorsTien Le, Hak Jin Lee, Hyung Jong Jin
JournalAnalytical biochemistry (Anal Biochem) Vol. 483 Pg. 4-6 (Aug 15 2015) ISSN: 1096-0309 [Electronic] United States
PMID25944416 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2015 Elsevier Inc. All rights reserved.
Chemical References
  • Deoxyribonuclease I
  • Peptide Hydrolases
Topics
  • Animals
  • Biochemistry (methods)
  • Cattle
  • Deoxyribonuclease I (metabolism)
  • Escherichia coli (metabolism)
  • Peptide Hydrolases (isolation & purification, metabolism)

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