Colloque

Presence of a DNase active at pH 5.4 in different tissues

Paul Lindsay

Michel Goudreau

Membre a labase

Paul Lindsay

Résumé du colloque

Normally the DNase activity in the high-speed supernatant fraction of rat liver is masked by the presence of very potent inhibitors of these enzymes, but nevertheless appreciable activity of DNase I could be demonstrated in this fraction by following up the increase in optical density at 260 mu in the Beckman DU-Spectrophotometer. Under the experimental conditions employed, maximum degradation of DNA by the enzyme present in the high-speed supernatant fractions occurs at pH 5.3 - 5.4, but under the same conditions, DNase II (Worthington) shows optimum activity at pH 4.8 - 5.0, which perhaps suggests the presence of a different DNase.