Enhancement of assays of activities of endonucleases on defined substrates by Poisson and non-Poisson combinatoric analysis.

Assay of endonuclease activity, as performed in most laboratories, depends upon change in form of small, defined substrate molecules, with a secondary computation required to obtain a determination of enzyme activity. We now explore the assumptions inherent in these computations and provide a series of equations that permit more accurate determinations of enzyme activity from assays of this type. These equations allow information to be obtained not only from substrate fractions left uncleaved by the endonuclease, upon which conventional systems rely, but also from products cleaved by the enzyme. Some information yielded by these equations is unobtainable using conventional methods of analysis.