Second, multiple-turnover experiments showed a burst of product formation, indicating that a step after chemistry is partially rate-limiting for MtATP-PRT.
Multiple-turnover experiments were performed at 30 °C in 0.1 M sodium phosphate buffer (pH 6.8) with 1% (v/v) acetonitrile.
These kinetic parameters are almost identical to those observed in the multiple-turnover experiments, suggesting that the same step is rate-limiting for single-turnover and multiple-turnover conditions.
To measure the affinity of AlkA for binding to the abasic product and undamaged DNA, we performed multiple-turnover experiments with mixtures of the 19TεC substrate and 25-mer DNA competitors that either contained a single abasic site or were undamaged.
The experiments of substrate specificity using several substrates were performed under multiple turnover conditions using 100 nM HDV ribozyme and 1 µM substrate.
We performed time course experiments to monitor the progression of intermolecular strand-joining reactions under multiple turnover conditions using a 5'-FAM-labeled 31-mer RNA and a 17-mer 5'-adenylated DNA adapter.
Under a multiple turnover condition, both performed well at 37°C, showing the kcat of 1 and 0.26 min−1, respectively.
Turnover experiments were performed using RGC5 cells, as well as the low and high expressers.
Turnover experiments showed that the endogenous optineurin was relatively short-lived, with a half-life of approximately 8 hours.
