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The purification of exonuclease I from Escherichia coli by affinity chromatography.

Abstract Escherichia coli exonuclease I has been purified to apparent homogeneity by affinity chromatography. The enzyme has been shown to be exonuclease I by examination of its catalytic and antigenic properties. Its activity is greatly reduced in strains harboring X onA or sbcB mutations. By analysis of acrylamide gels, the enzyme prepared by this method has an apparent molecular weight of 140,000, the protein being a dimer of 70,000 molecular weight subunits.