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Measuring RNase Activity A Real-time Kinetic Analysis

Recently, Ambion introduced the RNaseAlert QC System, a quantitative fluorometric high-throughput assay for the detection of contaminating RNases. The assay consists of an oligonucleotide substrate that contains a fluorophore on one end and a quencher on the other. Once cleaved by RNase, the fluor and quencher are separated. When excited with 490 nm light, the fluor emits a bright green signal that can be quantitated with a fluorometer (Figure 1).

Figure 1. Schematic of the RNaseAlert QC System.

Are Your Enzyme Units Uniform?

During routine protein purification some proportion of the enzyme population is inevitably inactivated. Therefore, the proportion of active enzyme is routinely quantitated by measuring the specific activity, the amount of active enzyme per mg of the total protein. In 1950, M. Kunitz developed the first spectrophotometric assay for measuring DNase I activity. The assay was based on the increase in A260 at pH 5.0 and 25C caused by the degradation of a DNA substrate. Kunitz also recognized that the rate of increase of A260 under the proper conditions, is both linear and constant and that the linear rates were proportional to the concentration of the active enzyme.

The Kunitz unit has since become the standard unit of measurement for enzymatic activity. However, the original Kunitz assay was performed under conditions that are not optimal for many enzymes, so most manufacturers have developed their own unit assays. Therefore, it is important to look closely at both t
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