DT-diaphorase Mutation and Enzymatic Activity
Author Information
Author(s): Misra V, Grondin A, Klamut H J, Rauth A M
Primary Institution: Department of Medical Biophysics, University of Toronto and Division of Experimental Therapeutics, Ontario Cancer Institute
Hypothesis
The study investigates the relationship between the genotypic status of a DT-diaphorase point mutation and its enzymatic activity.
Conclusion
The genotypic status is a reliable initial estimate of DT-diaphorase activity.
Supporting Evidence
- A common C to T nucleotide substitution in DT-diaphorase cDNA has been associated with protein instability and reduced catalytic activity.
- The study included a unique strain that is heterozygous for the polymorphism yet has undetectable enzymatic activity.
- The research confirmed that genotypic status correlates with enzymatic activity.
Takeaway
Scientists looked at how a specific gene change affects a protein's ability to work, finding that the gene type can help predict how well the protein functions.
Methodology
The study used a PCR-RFLP assay to assess enzymatic activity in human skin fibroblast strains.
Participant Demographics
Normal human skin fibroblast strains.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website