PARP-1 is a nuclear enzyme involved in a range of activities associated with DNA metabolism, playing a key role in maintaining the integrity of DNA and chromatin
structure. As such, this enzyme is likely to provide a useful target when using a rationale drug design approach to develop pharmaceutical reagents including cancer
therapeutics. A major obstacle to this work however is that our knowledge of the relationship between structure and function of PARP-1 is rather limited. Structure - function studies of enzymes typically require the application of techniques for producing reasonable quantities of high quality protein. To this end, this thesis describes the development of a rapid and relatively simple approach to producing and purifying PARP-1.