Abstract
This chapter describes the assay method of adenine phosphoribosyltransferase (APRT) enzyme. Human APRT catalyzes the magnesium-dependent transfer of the ribose-5-phosphate moiety of 5-phosphoribosyl-l-pyrophosphate (PP-ribose-P) to the 9 position of the purine base adenine to form adenosine-5'-monophosphate (AMP). Human APRT activity is found exclusively in the cytoplasm while in bacteria, APRT activity appears to be loosely associated with the cell membrane in the periplasmic space. Human APRT activity is assayed by a variety of radiochemical techniques. These techniques differ primarily by the procedure utilized to separate the radioactive purine substrate––adenine––from the product–– AMP. Each technique may have advantages depending on the specific purpose for assaying the enzyme. The monovalent cation sodium (Na + ) and the anions sulfate, succinate, and citrate are also inhibitors of APRT activity. Depending on the source of APRT enzyme, divalent metal ions and sulfhydryl binding agents are shown to inhibit APRT activity.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call